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Небесная энциклопедия

Космические корабли и станции, автоматические КА и методы их проектирования, бортовые комплексы управления, системы и средства жизнеобеспечения, особенности технологии производства ракетно-космических систем

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Мониторинг СМИ

Мониторинг СМИ и социальных сетей. Сканирование интернета, новостных сайтов, специализированных контентных площадок на базе мессенджеров. Гибкие настройки фильтров и первоначальных источников.

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Форма поиска

Поддерживает ввод нескольких поисковых фраз (по одной на строку). При поиске обеспечивает поддержку морфологии русского и английского языка
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Применить Всего найдено 726. Отображено 100.
10-12-2009 дата публикации

УСТАНОВКА ДЛЯ ПОЛУЧЕНИЯ МАКРОПОРИСТЫХ ПОЛИМЕРНЫХ МАТЕРИАЛОВ

Номер: RU0000089522U1

1. Установка для получения макропористых полимерных материалов монолитного типа для создания биоаффинных сорбентов, содержащая реакционную форму в виде колонки или пластины, рабочую герметизированную камеру, сушильную камеру, ванну с жидкой средой, контейнеры с компонентами, контейнер для хранения полученного материала, отличающаяся тем, что она дополнительно оснащена лазерным излучателем, емкостью с инертным газом, вакуум-насосом, сообщенными магистралями с полостью рабочей герметизированной камеры, оснащена также камерой с источником ультрафиолетового излучения и камерой для выдержки полученного материала, соединенной с источником инертного газа, прибором контроля параметров полученного полимерного материла. 2. Установка по п.1, отличающаяся тем, что контейнеры заполнены исходными компонентами соответственно: контейнер с глицидилметакрилатом, контейнер с N-гидроксифталимидным эфиром акриловой кислоты, контейнер с этиленгликольдиметакрилатом, контейнер с порогенными растворителями и инициатором. 3. Установка по п.1, отличающаяся тем, что в качестве прибора контроля используют сканирующий электронный микроскоп. РОССИЙСКАЯ ФЕДЕРАЦИЯ (19) RU (11) 89 522 (13) U1 (51) МПК C08J 5/00 (2006.01) C08F 220/00 (2006.01) C07K 17/00 (2006.01) ФЕДЕРАЛЬНАЯ СЛУЖБА ПО ИНТЕЛЛЕКТУАЛЬНОЙ СОБСТВЕННОСТИ, ПАТЕНТАМ И ТОВАРНЫМ ЗНАКАМ (12) ОПИСАНИЕ ПОЛЕЗНОЙ МОДЕЛИ К ПАТЕНТУ (21), (22) Заявка: 2009126715/22, 13.07.2009 (24) Дата начала отсчета срока действия патента: 13.07.2009 (45) Опубликовано: 10.12.2009 (73) Патентообладатель(и): Учреждение Российской академии наук Институт высокомолекулярных соединений РАН (RU) U 1 8 9 5 2 2 R U Ñòðàíèöà: 1 ru CL U 1 Формула полезной модели 1. Установка для получения макропористых полимерных материалов монолитного типа для создания биоаффинных сорбентов, содержащая реакционную форму в виде колонки или пластины, рабочую герметизированную камеру, сушильную камеру, ванну с жидкой средой, контейнеры с компонентами, контейнер для хранения полученного ...

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17-05-2012 дата публикации

Recombinant protein of fibroblast growth factor having adhesive activity for stem cells and method for culturing stem cells using the same

Номер: US20120122156A1

The present invention relates to a recombinant protein of a fibroblast growth factor (FGF) having an adhesive activity for stem cells and a method for culturing stem cells using the same. More particularly, the present invention relates to a recombinant protein having an adhesive activity for stem cells by fusion of a polypeptide linker at amino terminal of FGF, and a method for culturing stem cells using immobilized FGF comprising: fixing the recombinant protein in a culture vessel with a hydrophobic surface using amino terminal of the polypeptide linker, adhering stem cells on the recombinant protein-fixed culture vessel, and culturing the stem cells.

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13-09-2012 дата публикации

Glucose sensor

Номер: US20120232251A1
Автор: Faaizah Khan, John Pickup
Принадлежит: KINGS COLLEGE LONDON

The invention relates to a glucose binding protein comprising amino acid mutations relative to the wild type sequence at the following positions: (i) H 152, (ii) A213; and (iii) L238 wherein the mutation at position H 152 is H152C. The invention further relates to such a glucose binding protein comprising the mutations H152C, A213R and L238S, in particular when linked to an environmentally sensitive dye such as badan.

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27-12-2012 дата публикации

Heteropeptides useful for reducing nonspecific adsorption

Номер: US20120329986A1
Принадлежит: UNIVERSITE DE MONTREAL

Reagents, kits, uses and methods useful for example fo decreasing nonspecific adsorption of biomolecules at the surface of a solid support are disclosed. Such reagents and methods, which are based on short heteropeptides, may be used to decrease nonspecific adsorption in for example biosensing applications.

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21-03-2013 дата публикации

PEPTIDES, CONJUGATES AND METHOD FOR INCREASING IMMUNOGENICITY OF A VACCINE

Номер: US20130071428A1
Принадлежит:

The present invention relates to conjugates comprising a peptide of at least 10 amino acid residues comprising the amino acid sequence GITELKKL for induction of potent humoral and cellular immune responses when administered to subjects having antibodies against tetanus toxoid. In one embodiment the invention relates to a prophylactic and therapeutic vaccine and in a further embodiment the invention relates to the treatment or prevention of cancer or an infectious disease. 1. A conjugate , comprising a peptide conjugated to an antigen , immunogen or to a vehicle comprising an antigen or immunogen , wherein the peptide comprises:(i) at least 10 amino acid residues of SEQ ID NO:3 that comprise the amino acid sequence GITELKKL; or,(ii) an amino acid sequence having at least 80% sequence identity with an amino acid sequence as provided under (i) and wherein the peptide, when subjected to serum samples from at least 10 human subjects that had been vaccinated with tetanus toxoid is in at least 50% of the serum samples bound by antibodies from the serum samples, as determined in a Tettox ELISA;wherein the peptide is not the tetanus toxin beta chain.2. The conjugate according to claim 1 , wherein the peptide comprises less than 100 amino acid residues.3. The conjugate according to claim 1 , wherein the antigen claim 1 , the immunogen or the vehicle comprising the antigen or immunogen is conjugated to the C-terminus of the peptide.4. The conjugate according to claim 1 , wherein 2 to 20 peptides are bound to the antigen claim 1 , immunogen or the vehicle comprising the antigen or immunogen.5. A pharmaceutical composition comprising a conjugate according .6. A method for prevention or treatment of cancer or an infectious disease in a subject claim 1 , comprising administering to a subject in need thereof a conjugate according to .7. (canceled)8. The method according to claim 6 , wherein the subject has antibodies against tetanus toxin or tetanus toxoid.9. The method according ...

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04-04-2013 дата публикации

Methods of binding TNF-alpha using Anti-TNF-alpha antibody fragment-polymer conjugates

Номер: US20130084302A1
Принадлежит:

Described are conjugates formed by an antibody fragment covalently attached to a nonproteinaceous polymer, wherein the apparent size of the conjugate is at least about 500 kD. The conjugates exhibit substantially improved half-life, mean residence time, and/or clearance rate in circulation as compared to the underivatized parental antibody fragment. Also described are conjugates directed against human vascular endothelial growth factor (VEGF), human p185 receptor-like tyrosine kinase (HER2), human CD20, human CD18, human CD11a, human IgE, human apoptosis receptor-2 (Apo-2), human tumor necrosis factor-α (TNF-α), human tissue factor (TF), human αβintegrin, human GPIIb-IIIa integrin, human epidermal growth factor receptor (EGFR), human CD3, and human interleukin-2 receptor α-chain (TAC) for diagnostic and therapeutic applications. 132-. (canceled)33. A method of binding a conjugate to a tumor necrosis factor α (TNF-α) polypeptide in a mammal comprising a TNF-α polypeptide , the method comprising administering to said mammal a conjugate consisting essentially of an antibody fragment covalently modified by one or two nonproteinaceous polymer molecules at a free sulfhydryl group of a cysteine residue within the hinge region of the antibody fragment ,wherein said antibody fragment is engineered to both (1) provide an unpaired cysteine within the hinge region, so as to provide said free sulfhydryl group, and (2) to avoid disulfide bridge formation between said cysteine and an amino acid in the opposite chain of said antibody fragment,wherein (a) the average actual molecular weight of each nonproteinaceous polymer molecule is at least 20 kD, (b) the conjugate binds the same antigen as the parental molecule that is not covalently modified by one or two nonproteinaceous polymer molecules, wherein the antibody fragment comprises an antigen binding site that binds to a human TNF-α polypeptide.34. The method of wherein the mammal suffers from Crohn's disease.35. The method of ...

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18-04-2013 дата публикации

MULTIVALENT GLYCOPEPTIDE CONSTRUCTS AND USES THEREOF

Номер: US20130095173A1

Glycopeptide conjugates comprising GM2 and/or Gb5 carbohydrate determinants, and methods of making and using such conjugates are disclosed. The immunogenicity of select glycopeptide conjugates is demonstrated. 2. The method of claim 1 , wherein the glycopeptide has five to seven occurrences of A.3. The method of claim 1 , wherein the glycopeptide has seven occurrences of A.4. The method of claim 1 , wherein the glycopeptide has six occurrences of A.5. The method of claim 1 , wherein the glycopeptide has five occurrences of A.6. The method of claim 5 , wherein each occurrence of A is different.8. The method of claim 7 , wherein each n is independently 3-5.9. The method of claim 8 , wherein each n is independently 3 or 5.10. The method of claim 1 , wherein wherein Lis not —O—(CHMe)- or —O—CH—.11. The method of claim 1 , wherein the therapeutically effective amount comprises an amount effective to inhibit tumor growth.12. The method of claim 1 , wherein the therapeutically effective amount comprises an amount effective to elicit antibodies that recognize at least one of the carbohydrate determinants13. The method of claim 12 , wherein the therapeutically effective amount comprises an amount effective to elicit antibodies that recognize each of the carbohydrate antigens.14. The method of claim 1 , wherein the therapeutically effective amount is an amount effective to treat one or more solid tumors.15. The method of claim 14 , wherein the cancer is breast or prostate cancer.16. The method of claim 14 , wherein the cancer is ovarian cancer.17. The method of claim 16 , wherein the cancer is peritoneal cancer.18. The method of claim 16 , wherein the cancer is cancer of the fallopian tube.19. The method of claim 14 , wherein the cancer is epithelial cancer.20. The method of claim 1 , wherein the subject is in clinical remission claim 1 , or where the subject has been treated by surgery claim 1 , has limited unresected disease.21. The method of claim 1 , wherein the ...

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25-04-2013 дата публикации

Medium, devices and methods

Номер: US20130098834A1
Автор: Jonas Axelsson
Принадлежит: JJK MEDICAL Ltd

A separation medium is provided, comprising at least one megalin polypeptide and/or at least one cubilin polypeptide immobilized on a support. Also provided are devices comprising the separation medium, as well as methods and uses employing the separation medium for extracorporeal removal of low molecular weight proteins, or fragments or derivatives thereof, from complex biological fluids.

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02-05-2013 дата публикации

Methods And Compositions For Cellular Imaging And Cancer Cell Detection Using Light Harvesting Conjugated Polymer-Biomolecular Conjugates

Номер: US20130109029A1
Принадлежит: NATIONAL UNIVERSITY OF SINGAPORE

The present invention relates to conjugated polyelectrolyte (CPE) or oligoelectrolyte (COE) compounds represented by general structural formulae (I)-(IV), or a salt thereof and methods of using these compounds to detect targets in samples. In particular, the methods include: (1) exposing a sample to a compound of structural formula (I), (II) or (IV) or a salt thereof, allowing the compound to bind to a target and detecting a signal produced by the compound; (2) functionalizing a solid support with a ligand, incubating the sample with a charged CPE or COE and detecting the fluorescence of the solid support and thereby detecting the target or (3) functionalizing a surface of a solid support with a charged ligand, thereby creating a charge on the surface of the solid support; incubating the ligand-functionalized solid support with a sample, whereupon binding of the target, the charge on the surface of the solid support switches; incubating the sample with CPE or COE that has a complementary charge to the charge of the target-bound surface; and detecting the fluorescence of the solid support and thereby detecting the target. The compounds of the present invention possess high photoluminescence quantum yields in biological media, low cytotoxicity, and excellent environmental stability and photostability and can be used in biosensor and bioimaging applications. 2. The compound of claim 1 , or a salt thereof claim 1 , wherein R′ and Rare each a cationic alkyl group or a cationic oligo or poly(ethylene oxide) group.3. The compound of claim 1 , or a salt thereof claim 1 , wherein R′ and Rare each a charged side group selected from the group consisting of —(CH)N(R)X claim 1 , —(OCHCH)N(R)X and —(CHCHO)CHCHN(R)X claim 1 , wherein Ris (C1-C6)alkyl claim 1 , n is an integer between 2 and 13 claim 1 , inclusive claim 1 , q is an integer between 1 and 12 claim 1 , inclusive claim 1 , and X is an anionic counterion.4. The compound of claim 1 , or a salt thereof claim 1 , wherein Ar ...

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02-05-2013 дата публикации

Support for protein immobilization, immobilized protein, and methods for producing the same

Номер: US20130109072A1

A support for enzyme immobilization is described, which is for immobilizing enzymes of various molecular sizes and also for, due to the modification of the surface silanol groups of porous silica particles, for immobilizing various kinds of enzymes, and enables the design of an immobilized enzyme, which exhibits an activity equivalent to that of the corresponding non-immobilized enzyme and withstands repeated use. A method for producing the support is also described. The support includes porous silica particles having an interparticle void structure therein, characterized in that the porous silica particles have a specific average particle size, a specific surface area, a specific pore volume, a specific pore size distribution and a specific porosity and have a substituent containing an organic group or an amino group on the surface thereof. An immobilized protein obtained by immobilizing a protein on the above support is also described.

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02-05-2013 дата публикации

METHODS OF MAKING A DIAGNOSTIC COMPOSITION AND COMPOSITIONS THEREFROM

Номер: US20130109837A1
Принадлежит: ACHIRA LABS PVT. LTD

In one aspect, the invention provides a method for making a hydrophilic-silk composition. The method includes providing at least one strand of silk fiber, treating the silk fiber with an alkaline solution to provide at least one strand of degummed silk fiber, and treating the degummed silk fiber with a treatment solution to provide a hydrophilic-silk drophilic-silk composition. The degummed silk fiber or the hydrophilic-silk composition is further immobilized with at least one reagent to make a silk-based diagnostic composition. The invention provides a silk-based diagnostic composition made by the method of the invention, and a diagnostic device that comprises the silk-based diagnostic composition. In another aspect, the invention provides a method of making a diagnostic device. The method includes providing at least one strand of a diagnostic-fiber composition, providing at least one strand of a hydrophobic-fiber composition, inter-weaving the at least one strand of the diagnostic-fiber composition and the at least one strand of the hydrophobic-fiber composition. In one embodiment, the diagnostic-fiber composition and the hydrophobic-fiber composition are both based on silk. 1. A method for making a reagent-immobilized silk-fiber , said method comprising:providing at least one strand of silk fiber;treating the at least one strand of silk fiber with an alkaline solution to provide at least one strand of de gummed silk fiber; andimmobilizing at least one reagent onto the at least one strand of degummed silk fiber to provide a reagent-immobilized silk-fiber.2. A method of making a silk-based diagnostic composition , wherein the method comprises:providing at least one strand of silk fiber;treating the at least one strand of silk fiber with an alkaline solution to provide at least one strand of de gummed silk fiber;treating the at least one strand of de gummed silk fiber with a treatment solution to provide a hydrophilic-silk composition; andimmobilizing at least one ...

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23-05-2013 дата публикации

FUNCTIONALIZATION OF AND USE OF FUNCTIONALIZED SECOND HARMONIC GENERATING NANOPROBES

Номер: US20130129628A1
Принадлежит: California Institute of Technology

Functionalized second harmonic nanoprobes for imaging samples and a method of using such probes to monitor the dynamics different processeses using a variety of imaging techniques are provided. The functionalized second harmonic generating (SHG) nanoprobes are comprised of various kinds of nanocrystalline materials that do not possess an inversion symmetry and therefore are capable of generating second harmonic signals that can then be detected by conventional two-photon microscopy, and are provided with functional surface modifications that allow for targeted imaging of a variety of biological and non-biological processes and structures such as cell signaling, neuroimaging, protein conformation probing, DNA conformation probing, gene transcription, virus infection and replication in cells, protein dynamics, tumor imaging and cancer therapy evaluation and diagnosis as well as quantification in optical imaging. 1. A method of functionalizing second harmonic generating probe nanostructure comprising:providing a probe nanostructure formed from a nanocrystalline material capable of exposing free surface hydroxyls, the probe nanostructure defining an outer surface and having no inversion symmetry such that it generates a second harmonic emission when radiated by an external excitation source;hydroxylating the probe nanostructure to form an activated outer surface thereof;attaching a plurality of modifying molecules having amine terminal groups to the hydroxylates of the activated outer surface of the probe nanostructure to form a functionalization platform on said outer surface of the probe nanostructure; andfunctionalizing the amine terminal groups of the functionalization platform with a plurality of functionalization molecules to form a functionalized probe nanostructure.2. The method of claim 1 , wherein the nanocrystalline material is selected from the group consisting of BaTiO claim 1 , SiC claim 1 , ZnO claim 1 , LiNbO claim 1 , KNbO claim 1 , KTiOPO claim 1 , Fe( ...

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23-05-2013 дата публикации

PEGYLATED C-PEPTIDE

Номер: US20130130973A1
Принадлежит: Cebix AB

The present invention relates to PEGylated C-peptide derivatives comprising at least one PEG group attached to the N-terminus, which exhibit improved pharmacokinetic and biological activity in vivo. 1. A method for administering PEGylated C-peptide to a patient in need thereof , comprising administering to the patient PEGylated C-peptide sufficient to produce an Cof PEGylated C-peptide between about 0.44 nM and about 12.2 nM.2. The method of claim 1 , wherein the Cof PEGylated C-peptide is between about 2.0 nM and about 5.9 nM.3. The method of claim 1 , wherein the Cof PEGylated C-peptide is between about 0.34 nM and about 9.0 nM.4. The method of claim 2 , wherein the Cof PEGylated C-peptide is between about 1.7 nM and about 4.9 nM.5. The method of claim 1 , wherein the Cof PEGylated C-peptide is between about 0.5 nM and about 14.5 nM.6. The method of claim 5 , wherein the Cof PEGylated C-peptide is between about 2.3 nM and about 6.7 nM.7. The method of claim 1 , wherein the Tof PEGylated C-peptide is between about 1.8 to about 3.3 days.8. The method of claim 1 , wherein the half-life of PEGylated C-peptide is between about 5.0 days and about 11.2 days.9. The method of claim 1 , wherein the AUCof PEGylated C-peptide is between about 3.1 nM·day and about 85 nM·day.10. The method of claim 9 , wherein the AUCof PEGylated C-peptide is between about 13.8 nM·day and about 41.5 nM·day.11. The method of claim 1 , wherein the volume of distribution of PEGylated C-peptide is between about 5.8 L and about 22 L.12. The method of claim 11 , wherein the volume of distribution of PEGylated C-peptide is between about 10 L and about 15 L.13. The method of claim 1 , wherein the clearance of PEGylated C-peptide is between about 0.8 L/day and about 2.2 L/day.14. The method of claim 13 , wherein the clearance of PEGylated C-peptide is between about 1.1 L/day and about 1.6 L/day.15. The method of claim 1 , wherein the degree of fluctuation of PEGylated C-peptide is between about 36% and ...

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23-05-2013 дата публикации

Peptide Derivatives for Biofunctionalization of Silicon Substrates and Their Applications

Номер: US20130131314A1
Принадлежит:

The present invention relates to the use of a peptide consisting of 5 to 30 amino acid residues comprising an amino acid sequence selected from LLADTTHHRPWT (SEQ ID NO: 1), SPGLSLVSHMQT (SEQ ID NO: 2), and the sequences presenting at least 80% identity with SEQ ID NO: 1 or SEQ ID NO: 2, for the funcfionalization of silicon substrate. The present invention also relates to the specific peptides as such, and to silicon substrates functionalized by the adsorption on their surface of such specific peptides. Finally, the present invention is also directed to a process for the preparation of such functionalized silicon substrates, and to articles comprising a silicon substrate according to the invention. 1. (canceled)2. (canceled)3. A peptide consisting of 5 to 30 amino acid residues , wherein said peptide comprises an amino acid sequence selected from LLADTTHHRPWT (SEQ ID NO: 1) , SPGLSLVSHMQT (SEQ ID NO: 2) , and the sequences presenting at least 80% identity with SEQ ID NO: 1 or SEQ ID NO: 2.4. A peptide according to claim 3 , wherein said peptide consists of a sequence selected from SEQ ID NO: 1 or SEQ ID NO: 2.5. A silicon substrate which is functionalized by the adsorption on its surface of a peptide as defined according to .6. A silicon substrate according to claim 5 , wherein the silicon substrate is a porous silicon substrate having pores diameters ranging from 15 nm to 200 nm.7. A silicon substrate according to claim 5 , wherein the silicon substrate is a n-doped silicon substrate functionalized by the adsorption on its surface of a peptide comprising SEQ ID NO: 1.8. A silicon substrate according to claim 5 , wherein the silicon substrate is a p-doped silicon substrate functionalized by the adsorption on its surface of a peptide comprising SEQ ID NO: 2.9. A silicon substrate according to claim 5 , wherein the peptide adsorbed on its surface is covalently coupled at one end to a biological ligand.10. A silicon substrate according to claim 9 , wherein the ...

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20-06-2013 дата публикации

TEMPLATE-DIRECTED ASSEMBLY OF RECEPTOR SIGNALING COMPLEXES

Номер: US20130157337A1
Принадлежит: THE UNIVERSITY OF MASSACHUSETTS

Transmembrane receptors in the signaling pathways of bacterial chemotaxis systems influence cell motility by forming noncovalent complexes with the cytoplasmic signaling proteins to regulate their activity. The requirements for receptor-mediated activation of CheA, the principal kinase of the chemotaxis signaling pathway, can be demonstrated using self-assembled clusters of a receptor fragment (CF) derived from the cytoplasmic domain of the aspartate receptor, Tar. Histidine-tagged Tar CF can be assembled on the surface of unilamellar vesicles via a lipid containing the Nickel-nitrilotriacetic acid moiety as a headgroup. The stability of such a complex can be controlled by the properties of the template including the size and composition, which can be used, for example, to vary the 2-dimensional concentration of receptor fragments. Surface-assembled CF is also found to serve as a substrate for receptor methylation, which is catalyzed by the receptor transferase. Since neither CheA activation nor CF methylation is observed in comparable samples in the absence of vesicles, it is concluded that surface-templating generates the organization among CF subunits required for biochemical activity. 145-. (canceled)46. An in vitro assembly for use in protein assays , said assembly comprising:a lipid membrane including a first lipid component; and a plurality of a first membrane-associated protein component, said first membrane-associated protein component having a binding affinity for said first lipid component and being coupled with said lipid membrane by interaction with said first lipid component to promote a two dimensional organization of said plurality of first membrane-associated protein component that mimics a natural organization of said first membrane-associated protein component on a cell membrane; wherein said first-membrane-associated protein component, when coupled with said lipid membrane, exhibits a greater biological function than the first membrane-associated ...

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20-06-2013 дата публикации

METHOD FOR SELECTING A CANDIDATE DRUG COMPOUND

Номер: US20130158232A1
Принадлежит:

The disclosure relates to the field of candidate drug testing and drug development. Described are methods for providing a compound composed of at least one molecule attached via at least two linkages to a molecular scaffold, the method comprising providing a scaffold comprising at least a first and a second reactive group; providing at least one molecule able to react with the at least first and second reactive group; and contacting the scaffold with at least one molecule to form at least two linkages between the scaffold and the molecule in a coupling reaction, wherein the formation of a linkage accelerates the formation of a consecutive linkage. The coupling reaction may be performed in solution, such as an aqueous solution. Furthermore, described is a method for selecting a candidate drug compound comprising providing a library of the compounds and determining the binding of a target molecule to the compounds. 120-. (canceled)21. A compound comprising at least two looped peptide structures attached via at least three thioether linkages to an aromatic or heteroaromatic molecule , wherein each of the at least three thioether linkages comprises a sulfur at a benzylic position on said aromatic or heteroaromatic molecule.22. The compound of claim 21 , wherein the aromatic or heteroaromatic molecule comprises a 5- or 6-membered aromatic or heteroaromatic ring.23. The compound of claim 21 , wherein each of the at least three thioether linkages is formed by reactinga halomethyl group on an aromatic or heteroaromatic ring withan SH functionality comprised within the peptide structure,thereby forming at least three thioether linkages, each comprising a sulfur at a benzylic position on said aromatic or heteroaromatic molecule.24. The compound of claim 23 , wherein the aromatic molecule is an arene.25. The compound of claim 21 , wherein each of the at least three thioether linkages is formed by reactingone of the halomethyl groups on a tris-, or tetrakis(halomethyl)- ...

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27-06-2013 дата публикации

Apolipoprotein nanodiscs with telodendrimer

Номер: US20130165636A1
Принадлежит: UNIVERSITY OF CALIFORNIA

The present invention provides a nanodisc with a membrane scaffold protein. The nanodisc includes a membrane scaffold protein, a telodendrimer and a lipid. The membrane scaffold protein can be apolipoprotein. The telodendrimer has the general formula PEG-L-D-(R) n , wherein D is a dendritic polymer; L is a bond or a linker linked to the focal point group of the dendritic polymer; each PEG is a poly(ethylene glycol) polymer; each R is and end group of the dendritic polymer, or and end group with a covalently bound hydrophobic group, hydrophilic group, amphiphilic compound, or drug; and subscript n is an integer from 2 to 20. Cell free methods of making the nanodiscs are also provided.

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08-08-2013 дата публикации

METHOD FOR PURIFYING ACTIVE POLYPEPTIDES OR IMMUNOCONJUGATES

Номер: US20130202626A1
Принадлежит: MEDIMMUNE, LLC

The present invention provides methods for isolating an active polypeptide or immunoconjugate by purification of a solution containing both the active polypeptide or immunoconjugate and an acidic variant thereof, such as a deamidated variant, using anion exchange chromatography. 1. (canceled)2. A method of producing a purified polypeptide from a solution comprising the polypeptide and an acidic variant of the polypeptide , wherein said acidic variant of the polypeptide results in an inhibition of potency of said polypeptide , the method comprising: (a) contacting the polypeptide with an anion exchange (AIEX) chromatography matrix; and (b) eluting the bound polypeptide from the AIEX chromatography matrix with a high salt buffer , thereby separating said polypeptide from the acidic variant and producing a purified polypeptide;{'i': 'Pseudomonas', 'wherein the polypeptide comprises an antibody or antigen binding fragment thereof that binds the cell surface receptor CD22 and a exotoxin, or variant thereof.'}3. (canceled)4. The method of claim 1 , wherein the AIEX matrix contains quaternary amine and tertiary amine ion exchange groups.5. The method of claim 4 , wherein the AIEX matrix contains a quaternary amino (Q) group.6. The method of claim 5 , wherein the AIEX matrix is Q sepharose.7. The method of any of claim 1 , wherein the polypeptide is eluted with a linear or step salt gradient.8. The method of claim 7 , wherein the polypeptide is eluted with a linear salt gradient that is from about 150 mM NaCl in Tris/HCl claim 7 , pH 8.0 to about 300 mM NaCl in Tris/HCl claim 7 , pH 8.0 claim 7 , from about 175 mM NaCl in Tris/HCl claim 7 , pH 8.0 to about 275 mM NaCl in Tris/HCl claim 7 , pH 8.0 claim 7 , or from about 192 mM NaCl in Tris/HCl claim 7 , pH 8.0 to about 245 mM NaCl in Tris/HCl claim 7 , pH 8.0.911-. (canceled)12. The method of claim 1 , wherein between about 75 to about 99% claim 1 , about 80% claim 1 , about 85% claim 1 , about 90% claim 1 , about 95% claim ...

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15-08-2013 дата публикации

SUBSTRATE FOR IMMOBILIZING FUNCTIONAL SUBSTANCES AND METHOD FOR PREPARING THE SAME

Номер: US20130210111A1
Принадлежит: TEMASEK POLYTECHNIC

A substrate having compounds disposed thereon for immobilizing a functional molecule, each compound having a chain including: a moiety R that is chemically coupled to the substrate, the moiety R being selected from the group consisting of an ether, ester, carbonyl, carbonate ester, thioether, disulfide, sulfinyl, sulfonyl, and carbonothioyl; and an epoxide-containing moiety that is coupled to the moiety R by a linker including at least one nucleophilic group. Methods of preparing the substrate and use of the substrate are also disclosed 121-. (canceled)23. The method as claimed in claim 22 , further comprising the step of applying a substantially homogenous mixture of stabilizing additives to the surface of the substrate wherein said additives are selected to stabilize said functional molecule.24. The method as claimed in claim 23 , wherein the step of applying the substantially homogenous mixture of additives comprises evaporating a solvent of a solution of said additives onto the substrate.25. The method as claimed in claim 23 , wherein the stabilizing additives are selected from the group consisting of a sugar claim 23 , an organic acid claim 23 , an amino acid claim 23 , a sugar acid and a thiol.26. A method of preparing a substrate comprising immobilized functional molecules claim 23 , the method comprising the steps of:(i) providing electrophilic compounds coupled to the surface of the substrate;(ii) allowing the electrophilic compounds to undergo a nucleophilic substitution reaction to provide a nucleophilic group thereon and thereby increase the nucleophilicity of the substrate surface;(iii) allowing the nucleophilic group to undergo a nucleophilic substitution reaction with another electrophilic compound to provide an electrophilic group on the substrate surface and thereby increase the electrophilicity of the substrate;each electrophilic compound from step (iii) being coupled to said functional molecules, wherein the functional molecules comprise enzymes ...

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05-09-2013 дата публикации

ENGINEERED POLYPEPTIDE CONJUGATES AND METHODS FOR MAKING THEREOF USING TRANSGLUTAMINASE

Номер: US20130230543A1
Принадлежит:

The present invention provides engineered polypeptide conjugates (e.g., antibody-drug-conjugates, toxin-(biocompatible polymer) conjugates, antibody-(biocompatible polymer) conjugates, and bispecific antibodies) comprising acyl donor glutamine-containing tags and amine donor agents. In one aspect, the invention provides an engineered Fc-containing polypeptide conjugate comprising the formula (Fc-containing polypeptide)-T-A, wherein T is an acyl donor glutamine-containing tag engineered at a specific site or comprises an endogenous glutamine made reactive by the Fc-containing polypeptide engineering, wherein A is an amine donor agent, and wherein the amine donor agent is site-specifically conjugated to the acyl donor glutamine-containing tag or the endogenous glutamine. The invention also provides methods of making engineered polypeptide conjugates using transglutaminase. 1. An engineered Fc-containing polypeptide conjugate comprising the formula: (Fc-containing polypeptide)-T-A ,wherein T is an acyl donor glutamine-containing tag engineered at a specific site or comprises an endogenous glutamine (Q) made reactive by the Fc-containing polypeptide engineering;wherein A is an amine donor agent; wherein the amine donor agent is site-specifically conjugated to the acyl donor glutamine-containing tag or the endogenous glutamine at a carboxyl terminus, an amino terminus, or at an another site in the Fc-containing polypeptide, and wherein the acyl donor glutamine-containing tag comprises an amino acid sequence XXQX (SEQ ID NO:1), wherein X is any amino acid.2. The engineered Fc-containing polypeptide conjugate of claim 1 , wherein the acyl donor glutamine-containing tag is not spatially adjacent to a reactive Lys in the Fc-containing polypeptide.3. (canceled)4. An engineered Fc-containing polypeptide conjugate comprising the formula: (Fc-containing polypeptide)-T-A claim 1 , wherein T is an acyl donor glutamine-containing tag engineered at a specific site or comprises an ...

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12-09-2013 дата публикации

Sensor for Detecting Hydrogen Peroxide

Номер: US20130233729A1

The present invention relates to a sensor for detecting hydrogen peroxide, comprising: (a) a gold (Au) nanoparticle conjugated with a conducting oxide substrate comprising a conduction oxide; (b) a cytochrome c immobilized on the gold nanoparticle. In the performance of the present sensor, current values are increased in parallel with increased hydrogen peroxide concentration. Such performance enables to easily analyze the presence or concentration of hydrogen peroxide. 1. A sensor for detecting hydrogen peroxide , comprising: (a) a gold (Au) nanoparticle conjugated with a conducting oxide substrate comprising a conduction oxide; (b) a cytochrome c immobilized on the gold nanoparticle.2. The sensor according to claim 1 , wherein the conducting oxide is selected from the group consisting of a indium-tin oxide claim 1 , a indium-zinc oxide claim 1 , a tin oxide claim 1 , a zinc oxide claim 1 , a copper-aluminum oxide claim 1 , a copper-gallium oxide claim 1 , a copper-scandium oxide claim 1 , a copper-chrome oxide claim 1 , a copper-indium oxide claim 1 , a copper-yttrium oxide and a silver-indium oxide.3. The sensor according to claim 2 , wherein the conducting oxide is the indium-tin oxide.4. The sensor according to claim 1 , wherein the gold nanoparticle is indirectly conjugated with the conducting oxide substrate through a sulfhydryl group introduced to the surface of the conducting oxide substrate.5. The sensor according to claim 1 , wherein cytochrome cis indirectly immobilized on the gold nanoparticle through an amino group introduced to the surface of the gold nanoparticle.6. The sensor according to claim 1 , wherein the sensor further comprises a counter electrode and a reference electrode.7. The sensor according to claim 1 , wherein the sensor has a detection limit of 0.3-0.8 μM.8. The sensor according to claim 1 , wherein the sensor reaches a steady-state current in less than 10 sec.9. A method for detecting hydrogen peroxide in a sample claim 1 , ...

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12-09-2013 дата публикации

NK-1 Receptor Mediated Delivery of Agents to Cells

Номер: US20130236966A1
Принадлежит: The University of Chicago

Provided herein are conjugates including a targeting vehicle coupled to an agent. The targeting vehicle includes a tachykinin receptor ligand and a reactive moiety. Conjugates including a tachykinin receptor ligand attached to an antibody or fragment thereof that is specific for an intracellular target are also provided. Also provided are methods of delivering agents to cells expressing tachykinin receptors, methods of delivering antibodies or fragments thereof to an intracellular extra-endosomal target, and methods of arresting cell growth or introducing cell death of a cancer cell. 1. A conjugate having the structure:{'br': None, 'P-M-C-Ab,'}wherein P is a tachykinin receptor ligand or a variant thereof; M is a reactive moiety attached to or near the N-terminus of P; C is an optional crosslinker; and Ab is an antibody or fragment thereof specific for an intracellular target and is attached to M or C, if present.2. The conjugate of claim 1 , wherein the intracellular target is an extra-endosomal target.3. (canceled)4. The conjugate of claim 1 , wherein P is an NK-1 receptor ligand.5. The conjugate of claim 1 , wherein P comprises a ligand selected from the group consisting of SEQ ID NO: 1 claim 1 , SEQ ID NO: 2 claim 1 , SEQ ID NO: 3 claim 1 , SEQ ID NO: 4 claim 1 , SEQ ID NO: 5 claim 1 , and SEQ ID NO: 6.6. The conjugate of claim 1 , wherein M is maleimide.718-. (canceled)19. A method of delivering an antibody or a fragment thereof to a cell expressing a NK-1 claim 1 , NK-2 or NK-3 receptor comprising contacting the cell with the conjugate of claim 1 , wherein the antibody or fragment thereof is capable of binding to an intracellular target in the cell.20. The method of claim 19 , wherein the target is extra-endosomal.21. The method of claim 19 , wherein the antibody or antibody fragment is a synthetic antibody fragment (sAB).22. The method of claim 19 , wherein the antibody or antibody fragment is capable of reducing claim 19 , inhibiting or enhancing the ...

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19-09-2013 дата публикации

PROTEOGLYCAN-BONDED FIBER PRODUCT AND METHOD OF MANUFACTURING SAME

Номер: US20130245239A1
Автор: TAKI Takao
Принадлежит: OTSUKA PHARMACEUTICAL CO., LTD.

An objective is to provide fiber products having smooth texture and excellent softness, and in addition, excellent durability. A proteoglycan-bonded fiber product including a fiber to which a proteoglycan is covalently bonded is provided. 1. A proteoglycan-bonded fiber product comprising a fiber to which a proteoglycan is covalently bonded.2. The proteoglycan-bonded fiber product of claim 1 , wherein the fiber is a cellulose-based fiber.3. The proteoglycan-bonded fiber product of claim 2 , wherein the covalent bond is formed by a reaction of:(a) an amino group of a core protein of the proteoglycan; and(b) an aldehyde group of at least one acyclic glucose constituting the cellulose-based fiber.4. The proteoglycan-bonded fiber product of claim 1 , wherein the proteoglycan is aggrecan.5. A method for manufacturing a proteoglycan-bonded fiber product claim 1 , comprising the step of covalently bonding a proteoglycan to a fiber.6. The method of claim 5 , wherein the step of covalently bonding a proteoglycan to a fiber includes the sub-steps of:(1) treating a cellulose-based fiber with an oxidant to form an aldehyde group on a glucose molecule constituting the cellulose fiber; and(2) reacting the cellulose-based fiber having the aldehyde group obtained by step (1) with the proteoglycan in the presence of a reducing agent.7. The method of claim 6 , further comprising the step of bonding claim 6 , one or more times claim 6 , an additional proteoglycan to the proteoglycan of the proteoglycan-bonded fiber product obtained by sub-step (2). The present invention relates to proteoglycan-covalently-bonded fiber products including a fiber to which a proteoglycan is covalently bonded, and to methods for manufacturing the products.Proteoglycans are glycoconjugates consisting of a core protein and glycosaminoglycans (mucopolysaccharides) attached thereto. Proteoglycans are the major components of cellular surfaces and extracellular matrices, and occur in skin tissue, cartilage tissue ...

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19-09-2013 дата публикации

Bio-Hybrid Material, Production Method Therefor, and Stent

Номер: US20130245240A1

Provided is a bio-hybrid material that does not cause elution of nickel ions and has an excellent endothelialization ability, a production method therefor, and a stent. The bio-hybrid material () used includes an alloy part () free of Ni, an organic acid () having two or more active esters, and a cytokine (). The alloy part () free of Ni forms an ester bond with the organic acid (), and the organic acid () and the cytokine () are immobilized via an amide bond. 2. The bio-hybrid material according to claim 1 , wherein the cytokine is one selected from a group consisting of VEGF claim 1 , EGF claim 1 , FGF claim 1 , HGF claim 1 , PDGF claim 1 , and BMP.3. The bio-hybrid material according to claim 1 , wherein the organic acid having two or more active ester groups is one selected from a group consisting of citric acid claim 1 , tartaric acid claim 1 , malic acid claim 1 , succinic acid claim 1 , oxalacetic acid claim 1 , cis-aconitic acid claim 1 , 2-ketoglutaric acid claim 1 , maleic acid claim 1 , fumaric acid claim 1 , and any derivative thereof.4. The bio-hybrid material according to claim 1 , wherein the alloy part free of Ni is an alloy containing two or more elements selected from a group consisting of Fe claim 1 , Mo claim 1 , Co claim 1 , and Cr.5. The bio-hybrid material according to claim 4 , wherein the alloy contains nitrogen in an amount ranging from 0.5 wt % to 1 wt %.6. A production method of a bio-hybrid material comprising the steps of:surface-treating, in which hydrophilic surface treatment is performed on an alloy part free of Ni;organic acid-immobilizing, in which an organic acid having two or more active ester groups is immobilized on the alloy part free of Ni; andcytokine-immobilizing, in which a cytokine is immobilized on the organic acid.7. The production method of a bio-hybrid material according to claim 6 , wherein the hydrophilic surface treatment is UV irradiation treatment.8. The production method of a bio-hybrid material according to ...

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07-11-2013 дата публикации

Methods and Reagents for Preparing Multifunctional Probes

Номер: US20130295640A1
Принадлежит:

Multifunctional probes are synthesized in a single step using peptide scaffold-based multifunctional single-attachment-point reagents. To obtain multifunctional probes of the invention, a substrate (e.g., a nanoparticle, polymer, antibody, protein, low molecular weight compound, drug, etc.) is reacted with a multifunctional single-attachment-point (MSAP) reagent. The MSAP reagents can include three components: (i) a peptide scaffold, (ii) a single chemically reactive group on the peptide scaffold for reaction of the MSAP with a substrate having a complementary reactive group, and (iii) multiple functional groups on the peptide scaffold. The peptide scaffold can include any number of residues; however, for ease of synthesis and reproducibility in clinical trials, it is preferred to limit the residues in the peptide to 20 or less. The reagent can be prepared to yield a predetermined stoichiometric ratio of the functional groups on the scaffold such that the probe has a fixed stoichiometric ratio of the functional groups. 1. A reagent for preparing a multifunctional probe including a substrate , the reagent comprising:a peptide scaffold having a reactive group suitable for reacting with a complementary reactive group on the substrate;a first functional group attached to the scaffold; anda second functional group attached to the scaffold, the second functional group being different from the first functional group,wherein the peptide includes 20 or less residues.2. The reagent of wherein:the reagent is prepared to yield a predetermined stoichiometric ratio of the first functional group and the second functional group on the scaffold.3. The reagent of wherein:the reactive group of the scaffold is a single attachment point for the scaffold and the complementary reactive group of the substrate.4. The reagent of wherein:at least one of the first functional group and the second functional group is a chelate.5. The reagent of wherein:the chelate includes a magnetic material.6. ...

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12-12-2013 дата публикации

NANOPARTICLE MEDIATED GENE THERAPY, DIAGNOSTIC PRODUCTS AND THERAPEUTIC PRODUCTS FOR BREAST CANCER

Номер: US20130330279A1
Принадлежит: NNANOAXIS, LLC

The present disclosure provides compositions and methods of treating Breast Cancer. Disclosed is a nanoparticle paired to at least one of W genetic materials that suppress key regulators of fat synthesis (e.g. Rev-erb) to cause a predefined target cell types apoptosis or X predefined targeting moieties that cause predefined target cell types apoptosis and correspond to Y predefined target parameters associated with Z predefined target cell types in connection with treatment of at least one of the following breast cancer, glioblastoma, head and neck cancer, pancreatic cancer, lung cancer, cancer of the nervous system, gastrointestinal cancer, prostate cancer, ovarian cancer, kidney cancer, retina, cancer, skin cancer, liver cancer, genital. 1. A product comprising:a nanoparticle paired to at least one of W genetic materials that suppress key regulators of fat synthesis to cause at least one or more predefined target cell types apoptosis, decreased cell proliferation, increased apoptosis, or decreased angiogenesis; or the nanoparticle paired to X predefined targeting moieties that cause the at least one or more predefined target cell types apoptosis, decreased cell proliferation, increased apoptosis, or decreased, angiogenesis and correspond to Y predefined target parameters associated with Z predefined target cell types in connection with treatment of at least one of the following breast cancer, glioblastoma, head and neck cancer, pancreatic cancer, lung cancer, cancer of the nervous system, gastrointestinal cancer, prostate cancer, ovarian cancer, kidney cancer, retina cancer, skin cancer, liver cancer, genital-urinary cancer, or bladder cancer, wherein W, X, Y, and Z are integers.2. The product of claim 1 , wherein the nanoparticle is a biodegradable polymer.3. The product of claim 1 , wherein the nanoparticle is a poly(lactic-co-glycolic acid) biodegradable polymer epitaxially surrounded by a chitosan biodegradable material.4. The product of claim 3 , wherein the ...

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19-12-2013 дата публикации

BIOCONJUGATION USING BIFUNCTIONAL LINKERS

Номер: US20130338044A1
Автор: Liao Jiayu, Zheng Yongfeng
Принадлежит:

A bifunctional linker and method of use is provided that has a spacer molecule with a functional group on one end configured to couple to the surface of a substrate and a function group on the other end that is configured couple to a biomolecule and methods of use. The preferred bifunctional linker has a poly(ethylene glycol) spacer ranging from 3 to 20 ethylene glycol units that has a silane functional group to react with a substrate and an azide functional group that can couple to a biomolecule that includes an alkyne group. The preferred linker can produce an azide-derivatized glass surface in one step and the azide functional group of the spacer can in sequence conjugate with a biomolecule using click chemistry, which can be conducted at low temperature and in aqueous solution. 1. A surface modifying agent for the attachment of a biomolecule to a substrate , comprising:a spacer having first and second ends;a substrate surface conjugating functional group attached to the first end of said spacer and configured to couple with a substrate surface; anda biomolecule conjugating functional group attached to said second end of said spacer and configured to couple to a biomolecule.2. An agent as recited in claim 1 , wherein the substrate surface conjugating functional group attached to the first end of said spacer comprises an alkoxysilane functional group.3. An agent as recited in claim 2 , wherein the alkoxysilane functional group comprises a trialkoxysilane.4. An agent as recited in claim 3 , wherein the trialkoxysilane functional group comprises a triethyloxysilane functional group.5. An agent as recited in claim 1 , wherein the substrate surface conjugating functional group attached to the first end of said spacer is selected from the group consisting essentially of a dihydrogen phosphate group claim 1 , a thiol group and an alkyne group.6. An agent as recited in claim 1 , wherein the biomolecule conjugating functional group attached to the second end of the spacer ...

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19-12-2013 дата публикации

INSULIN-LIPID COMPLEX,PREPARATION METHOD THEREFOR, AND PREPARATION THEREOF

Номер: US20130338064A1

Provided are an insulin-lipid complex, a preparation method thereof, and a formulation thereof. The insulin-lipid complex is prepared by compounding insulin and a lipid material in an organic solvent system containing a low boiling point acid, and drying. The mass ratio of insulin to the lipid material is 1:3˜1:20. An oil solution of the insulin-lipid complex and vesicles containing insulin are further provided. 1. A insulin-lipid complex , wherein the insulin-lipid complex is composed of insulin and lipid material , the mass ratio of insulin to the lipid material being 1:3˜1:20.2. The insulin-lipid complex according to claim 1 , whereinsaid insulin is selected from the group consisting of natural insulin, porcine insulin, bovine insulin, recombinant human insulin and medium or long-acting insulin, and;said lipid material is selected from the group consisting of natural phospholipids, synthetic phospholipids, cholesterol, cholic acid and salts thereof.3. The insulin-lipid complex according to claim 2 , wherein said insulin is recombinant human insulin claim 2 , said lipid material is natural phospholipids claim 2 , and the mass ratio of insulin to the natural phospholipids is 1:5˜1:10.4. The insulin-lipid complex according to claim 1 , wherein said insulin-lipid complex contains at least one of antioxidants claim 1 , metal-chelators or protease inhibitors.5. The insulin-lipid complex according to claim 1 , wherein said insulin-lipid complex uses an organic solvent system containing a low boiling point acid as a complex solvent.6. The insulin-lipid complex according to claim 5 , wherein said low boiling point acid is selected from the group consisting of trifluoroacetic acid claim 5 , hydrogen chloride gas claim 5 , and a combination thereof claim 5 , and said organic solvent is the group consisting of methanol claim 5 , tetrahydrofuran claim 5 , DMSO claim 5 , chloroform claim 5 , dichloromethane claim 5 , and a combination thereof.7. An insulin-lipid complex oil ...

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16-01-2014 дата публикации

SUBSTRATE FOR IMMOBILIZING FUNCTIONAL SUBSTANCES AND METHOD FOR PREPARING THE SAME

Номер: US20140017761A1
Принадлежит: TEMASEK POLYTECHNIC

A substrate having compounds disposed thereon for immobilizing a functional molecule, each compound having a chain including: a moiety R that is chemically coupled to the substrate, the moiety R being selected from the group consisting of an ether, ester, carbonyl, carbonate ester, thioether, disulfide, sulfinyl, sulfonyl, and carbonothioyl; and an epoxide-containing moiety that is coupled to the moiety R by a linker including at least one nucleophilic group. Methods of preparing the substrate and use of the substrate are also disclosed. 1. A method of preparing a substrate comprising immobilized functional molecules , the method comprising the steps of:(i) Providing electrophilic compounds coupled to the surface of the substrate;(ii) Allowing the electrophilic compounds to undergo a nucleophilic substitution reaction to provide a nucleophilic group thereon and thereby increase the nucleophilicity of the substrate surface;(iii) Allowing the nucleophilic group to undergo a nucleophilic substitution reaction with another electrophilic compound to provide an electrophilic group on the substrate surface and thereby increase the electrophilicity of the substrate;each electrophilic compound from step (iii) being coupled to a functional molecule,wherein the functional molecule is selected from a group consisting of an affinity ligand, a chelator, a catalyst, an ion exchanger, a dye and an indicator.2. The method as claimed in claim 1 , wherein the substrate further comprising a coating disposed on said substrate claim 1 , the coating comprising a substantially homogenous mixture of stabilizing additives selected to stabilize said functional molecule claim 1 , wherein the stabilizing additives are selected from the group consisting of a sugar claim 1 , an organic acid claim 1 , an amino acid claim 1 , an a sugar acid.3. The method as claimed in claim 1 , wherein the functional molecule is chiral4. The method as claimed in claim 1 , wherein the functional molecule is a ...

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20-02-2014 дата публикации

METHOD OF PRODUCING FUNCTIONAL MOLECULE-CONTAINING SILICA NANOPARTICLES ON WHICH BIOMOLECULES ARE BONDED

Номер: US20140051186A1
Принадлежит: FURUKAWA ELECTRIC CO., LTD.

A method of producing functional molecule-containing silica nanoparticles on which a biomolecule is bonded, containing the steps of: 1. A method of producing functional molecule-containing silica nanoparticles on which a biomolecule is bonded , comprising the steps of:allowing silica nanoparticles containing a functional molecule and having a thiol group on the surface thereof to coexist with a linker molecule having a maleimido group and a carboxyl group in an aprotic solvent, thereby allowing formation of a thioether bond between the thiol group and the maleimido group, and obtaining functional molecule-containing silica nanoparticles on which the linker molecule is bonded; andallowing the functional molecule-containing silica nanoparticles on which the linker molecule is bonded to coexist with a carbodiimide and a biomolecule having an amino group in an aqueous solvent, thereby allowing formation of an amide bond between the carboxyl group active esterified by the carbodiimide, and the amino group of the biomolecule;wherein the method comprises the following steps for preparing the silica nanoparticles containing the functional molecule and having the thiol group on the surface thereof:mixing organoalkoxysilane having the functional molecule and tetraalkoxysilane in an ammonia-containing aqueous solvent to allow formation of silica core particles containing the functional molecule in the solvent, thereby obtaining a dispersion liquid of the core particles; andadding organoalkoxysilane having the thiol group and TEOS to the dispersion liquid obtained in the above step, thereby allowing formation of a shell layer on the silica core particles.2. A method of producing functional molecule-containing silica nanoparticles on which a biomolecule is bonded , comprising the steps of:allowing silica nanoparticles containing a functional molecule and having a thiol group on the surface thereof to coexist with a linker molecule having a maleimido group and a carboxyl group in ...

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01-01-2015 дата публикации

Functionalized graphene substrates

Номер: US20150004667A1
Принадлежит: NANOTECH BIOMACHINES, INC.

The present invention is generally directed to functionalized graphene substrates, methods of making such substrates and methods of using such substrates. In one aspect, the present invention provides a graphene substrate. The substrate comprises edge and non-edge regions, and organic or inorganic molecules are bound to the edge regions of the substrate. The organic or inorganic molecules are present on the substrate edges at a population greater than about one molecule per 10,000 nm. 1. A graphene substrate , wherein the substrate comprises edge and non-edge regions , and wherein organic or inorganic molecules are bound to the edge regions of the substrate , and wherein the organic or inorganic molecules are present on the substrate edges at a population greater than about one molecule per 10 ,000 nm.2. The graphene substrate according to claim 1 , wherein organic molecules are present on the substrate claim 1 , and wherein the organic molecules are selected from a group consisting of: antibodies; antibody fragments; aptamers; large molecule therapeutics; oligonucleotides; oligopeptides; oligopeptides claim 1 , proteins and small molecule therapeutics.3. The graphene substrate according to claim 2 , wherein the population is greater than about 10 molecules per 10 claim 2 ,000 nm.4. The graphene substrate according to claim 3 , wherein the organic molecules are selected from a group consisting of antibodies; antibody fragments; proteins; and claim 3 , aptamers.5. The graphene substrate according to claim 3 , wherein the organic molecules are selected from a group consisting of: large molecule therapeutics; oligonucleotides; oligopeptides; oligopeptides and small molecule therapeutics.6. The graphene substrate according to claim 4 , wherein the population is greater than about 50 molecules per 10 claim 4 ,000 nm.7. The graphene substrate according to claim 5 , wherein the population is greater than about 50 molecules per 10 claim 5 ,000 nm.8. The graphene substrate ...

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01-01-2015 дата публикации

Affinity Tag System

Номер: US20150005480A1
Принадлежит: UNIVERSITY COLLEGE DUBLIN

The present invention pertains to an affinity tag system for the immobilisation and/or purification of molecules such as biological or organic molecules. The invention provides EF-hand subdomains of calcium binding proteins, such as calbindin D9k, as affinity tags and affinity ligands for immobilising, detecting and/or for purifying molecules, particularly proteins. Also provided are methods utilising the affinity tag system of the invention, affinity matrices comprising EF-hand subdomain affinity ligands and fusion proteins comprising EF-hand subdomain affinity tags. 176-. (canceled)77. An affinity tag system for immobilizing a molecule , said system comprising:(i) an affinity matrix comprising a first EF-hand subdomain or fragment thereof attached to a substrate; and(ii) a molecule tagged with a second EF-hand subdomain or fragment thereof, wherein the molecule is immobilized at the substrate via the interaction between the first and second EF-hand subdomains or fragments thereof.78. The system of wherein the first EF-hand subdomain or fragment thereof is capable of binding to the second EF-hand subdomain or fragment thereof in the presence of calcium and/or wherein the affinity of binding between the first EF-hand subdomain and the second EF-hand subdomain is K=10 nM or less.79. The system of wherein the first EF-hand subdomain is selected from the group consisting of the EF-hand domains found in any calcium binding protein comprising two or more EF hands claim 77 , and wherein the EF-hand subdomain is capable of forming a binding pair with a second EF-hand subdomain claim 77 , in the presence of calcium.80. The system of wherein the first EF-hand subdomain is selected from:(i) a protein of human, bovine, murine or rat origin;(ii) the group of protein subdomains comprising the amino acid sequence of any one of SEQ ID NO: 3-18;(iii) the group of protein domains comprising an amino acid sequence with at least 85% sequence identity to any one of SEQ ID NO: 3-18;(iv) ...

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08-01-2015 дата публикации

COMPOSITION FOR EMBEDDED MICROBIAL CULTURE

Номер: US20150010980A1
Принадлежит: UPM-KYMMENE CORPORATION

Disclosed is a composition for embedded three-dimensional microbial culture, the composition including nanofibrillar cellulose and at least one nutrient source. Also disclosed is a method for the manufacture of a composition for embedded three-dimensional microbial culture, the method including the steps of providing nanofibrillar cellulose, mixing the nanofibrillar cellulose with water and at least one nutrient source and optional additives to obtain a mixture, and optionally drying the mixture. 120-. (canceled)21. A composition for embedded three-dimensional microbial culture , said composition comprising nanofibrillar cellulose and at least one nutrient source.22. The composition according to claim 21 , wherein the nanofibrillar cellulose is selected from plant derived nanofibrillar celluloses and microbial nanofibrillar celluloses.23. The composition according to claim 21 , wherein the nanofibrillar cellulose is selected from native nanofibrillar celluloses and chemically modified nanofibrillar celluloses.24. The composition according to claim 21 , wherein the nanofibrillar cellulose is native ion-exchanged nanofibrillar cellulose.25. The composition according to claim 21 , wherein the composition comprises 0.05-80 wt % of nanofibrillar cellulose.26. The composition according to claim 21 , wherein the composition comprises water and optional additives.27. The composition according to claim 21 , wherein the composition is in the form of hydrogel or powder.28. A method for the manufacture of a composition for embedded three-dimensional microbial culture claim 21 , said method comprising the steps of providing nanofibrillar cellulose claim 21 , mixing said nanofibrillar cellulose with water and at least one nutrient source and optional additives to obtain a mixture claim 21 , and optionally drying said mixture.29. The method according to claim 28 , wherein the nanofibrillar cellulose is selected from plant derived nanofibrillar celluloses and microbial ...

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14-01-2016 дата публикации

Multi-analyte assay

Номер: US20160011185A1
Принадлежит: Verax Biomedical Inc

The present invention is directed to devices and methods using pan-generic antibodies to detect bacteria in a sample. The invention relates to binding assays, especially immunoassays, utilizing a multivalent binding agent immobilized on a particle. The invention also relates to the surprising discovery that increasing the size of the particles improves the sensitivity of the screen. The invention provides, inter alia, a lateral flow device for detecting bacteria in a sample, the device comprising a flow path for the sample and further comprising a pan-generic binding agent specific for other or more bacterial antigens, wherein the pan-generic binding agent is immobilized via a linker on a population of particularly-sized detectable particles; and a capture binding agent that captures the population of particles bound to bacterial antigens, wherein the capture binding agent is immobilized on the flow path, and wherein the population of detectable particles are disposed along the flow path such that the sample contacts the population of detectable particles before contacting the capture binding agent.

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10-01-2019 дата публикации

Quantitative flagellar fluorescent markers and standards

Номер: US20190011368A1
Автор: Pinfen Yang, Yi Liu
Принадлежит: Marquette University

Disclosed are fluorescent markers that include a known number of copies of a fluorescently-labeled protein regularly interspersed along the length of the fluorescent marker. The fluorescent markers may be used to quantify fluorescently-labeled samples in fluorescent microscopy.

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19-01-2017 дата публикации

BRAIN SPECIFIC EXOSOME BASED DIAGNOSTICS AND EXTRACORPOREAL THERAPIES

Номер: US20170014450A1
Принадлежит: EXOSOME SCIENCES, INC.

Disclosed are methods, compositions, devices, and kits for the isolation of brain-specific exosomes. Specifically, methods, compositions, devices, and Unbound kits comprising an isolated brain-specific extracellular vesicle or exosome joined to a first binding agent that is specific for tau, β-amyloid, SlOO β, neuron-specific enolase, glycoprotein A2B5, CD133, NQ01, synaptophysin, neuronal nuclei, MAB 1569, polysialic acid-neural cell adhesion molecule (PSA-NCAM), or neurogenic differentiation 1 (NeuroD or Beta2), or glycosylated or phosphorylated forms of these molecules, are provided. 160-. (canceled)61. A diagnostic device , comprising:a substrate comprising a sample reservoir, wherein said sample reservoir is configured to receive an amount of a biological sample and said sample reservoir comprises an amount of one or more mobilizable labeled antibodies or binding fragments thereof specific for tau, glycosylated tau, phosphorylated tau, β-amyloid, glycosylated β-amyloid, or phosphorylated β-amyloid, or a fragment thereof or any combination thereof;an absorbent material in fluid communication with said substrate distal from said sample reservoir;a lectin immobilized to said substrate at a test zone, wherein said test zone is in fluid communication with said sample reservoir and said absorbent material;a first amount of a protein comprising tau, glycosylated tau, phosphorylated tau, β-amyloid, glycosylated β-amyloid, or phosphorylated β-amyloid, or a fragment thereof or any combination thereof immobilized to said substrate at a first control/standard zone, wherein said first control/standard zone is in fluid communication, with said sample reservoir and, wherein the first amount of protein in the first control/standard zone is an amount detectable by said mobilizable labeled antibodies or binding fragments thereof in a biological sample obtained from a healthy subject; and/ora second amount of a protein comprising tau, glycosylated tau, phosphorylated tau, β- ...

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21-01-2016 дата публикации

ADSORBENT

Номер: US20160017059A1
Принадлежит: Hitachi, Ltd.

An adsorbent of the present invention includes a support; and a protein having an adsorption site for adsorbing a target substance, in which the protein includes a reversible binding site and a covalent binding site, the support includes an orientation-controlling site forming a reversible bond with the reversible binding site, and an immobilization site forming a covalent bond with the covalent binding site, the covalent binding site includes a nucleophilic functional group, and the immobilization site includes a functional group capable of reacting with the nucleophilic functional group by a nucleophilic substitution or a nucleophilic addition. Thus, it is possible to provide an adsorbent in which the utilization efficiency of the adsorption site of the protein is improved. As a result, the protein amount can be reduced, and the step for storing a culture solution can be simplified due to the faster purification step.

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16-01-2020 дата публикации

NANOPARTICLES ADSORBED WITH GLIADIN MOLECULES

Номер: US20200017604A1
Принадлежит: UNIVERSITY OF TECHNOLOGY SYDNEY

The present disclosure generally relates to nanoparticles adsorbed with gliadin molecules. In addition, the present disclosure relates to methods of preparing the nanoparticles adsorbed with gliadin molecules and methods of using said nanoparticles including detecting anti-gliadin 5 antibodies in a sample, diagnosing gluten-related disorders, and other applications. 140.-. (canceled)41. A method of preparing a nanoparticle adsorbed with a gliadin molecule , the method comprising:(a) dissolving a gliadin molecule in a solution comprising a cationic surfactant and a polar protic solvent;(b) adding a nanoparticle to the solution obtained in step (a) to form a mixture; and(c) isolating a nanoparticle adsorbed with a gliadin molecule from the mixture obtained in step (b).42. The method according to claim 41 , wherein the cationic surfactant is cetyl trimethylammonium bromide and/or wherein the polar protic solvent is isopropanol.43. The method according to :(i) further comprising heating the solution obtained in step (a) to a temperature from about 40° C. to about 80° C.; and/or(ii) further comprising filtering the solution prior to step (b); and/or(iii) further comprising resuspending the nanoparticle in a solution prior to step (c); and/or(iv) further comprising incubating the mixture obtained in step (b) for at least 30 minutes prior to step (c), such as for about 60 minutes prior to step (c); and/or(v) wherein step (c) comprises centrifugation.44. A kit for use in detecting an anti-gliadin antibody claim 41 , the kit comprising a nanoparticle adsorbed with a gliadin molecule claim 41 , wherein the gliadin molecule retains sufficient conformational similarity to naturally occurring gliadin to be bound by an immunoglobulin that is capable of binding specifically to naturally occurring gliadin claim 41 , and a buffer.45. A method of detecting an anti-gliadin antibody in a sample claim 41 , the method comprising(i) contacting the sample of a body fluid obtained from an ...

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17-02-2022 дата публикации

CARRIER FOR ENZYME IMMOBILIZATION USE, AND IMMOBILIZED ENZYME

Номер: US20220049237A1
Принадлежит:

This invention provides a novel carrier for enzyme immobilization and an immobilized enzyme. The carrier for enzyme immobilization according to an embodiment comprises a porous material and cellulose that has an amino group-containing substituent at an anomeric position and is immobilized on the porous material. The immobilized enzyme contains the carrier for enzyme immobilization and an enzyme immobilization on the cellulose. The carrier for enzyme immobilization is obtained by adding an acid to an aqueous solution in which cellulose having an amino group-containing substituent at an anomeric position is dissolved in an aqueous alkaline solution to deposit the cellulose in the presence of a porous material. The immobilized enzyme is obtained by immobilizing an enzyme on the cellulose. 1. A carrier for enzyme immobilization comprising a porous material and cellulose , the cellulose having an amino group-containing substituent at an anomeric position and being immobilized on the porous material.3. The carrier for enzyme immobilization according to claim 1 , wherein the porous material comprises a fibrous material.4. An immobilized enzyme comprising the carrier for enzyme immobilization of claim 1 , and an enzyme that is immobilized on the cellulose.5. A method for producing a carrier for enzyme immobilization claim 1 , comprisingadding an acid to an aqueous solution in which cellulose having an amino group-containing substituent at an anomeric position is dissolved in an aqueous alkaline solution to deposit the cellulose in the presence of a porous material to thereby immobilize the cellulose on the porous material.6. A method for producing an immobilized enzyme claim 1 , comprisingadding an acid to an aqueous solution in which cellulose having an amino group-containing substituent at an anomeric position is dissolved in an aqueous alkaline solution to deposit the cellulose in the presence of a porous material to thereby immobilize the cellulose on the porous ...

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11-02-2016 дата публикации

Method for the site-specific covalent cross-linking of antibodies to surfaces

Номер: US20160041157A1

This invention relates to conjugate antibody, drug and nanoparticle compositions and methods of generating the same. This invention further relates to methods of using same for imaging, diagnosing or treating a disease. 1. A conjugate composition comprising a recombinant protein comprising an amino acid that permits specific binding to an immunoglobulin Fc region.2. The composition of claim 1 , wherein said immunoglobulin is IgG.3. The composition of claim 1 , wherein said recombinant protein is a recombinant bacterial protein.4. The composition claim 3 , wherein said recombinant bacterial protein is protein Z.54. The composition of any one of - claims 1 , wherein said amino acid is a UV-active non-natural amino acid.6. The composition of claim 5 , wherein said amino acid is benzoylphenylalaine (BPA).7. The composition of claim 6 , wherein said recombinant protein is a fusion protein.8. The composition of claim 7 , wherein said fusion protein comprises protein Z and an additional polypeptide.9. The composition of claim 8 , wherein said recombinant protein further comprises a moiety for expressed protein ligation.10. The composition of claim 9 , wherein said moiety is an intein-MPB group or a sortase-Hisx6 group.11. The composition of claim 1 , wherein said recombinant protein is attached to a peptide via expressed protein ligation.12. The composition of claim 11 , wherein said peptide is attached to an additional polypeptide of interest via a crosslinker.13. The composition of claim 11 , wherein said peptide comprises a chemical moiety that permits chemical binding to a corresponding chemical group.14. The composition of claim 13 , wherein said chemical binding is click chemistry or maleimide chemistry.1514. The composition of any one of - claims 11 , wherein said recombinant protein specifically attached in the proper orientation to a surface claims 11 , polypeptide claims 11 , a nanoparticle claims 11 , or a drug via said click chemistry.1614. The composition of ...

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11-02-2016 дата публикации

Peptide with gold binding and egfr receptor affinity and same attached to gold nanostructure

Номер: US20160041188A1
Принадлежит: University of Missouri System

An embodiment of the invention is a peptide comprising four domains, wherein domain I consists of thioctyl or monocytl, domain II consists of 2 to 3 positively charged amino acids selected from the group consisting of lysine and arginine, domain III consists of a dimeric ethylene unit; and domain IV comprises the peptide with SEQ ID No. 1 or a sequence having at least 90% identity to SEQ ID No. I. The peptide is preferably attached to a gold nanostructure, preferably a gold nanorod to provide an EFGR kit. An EFGR detection kit of the invention employs a gold nanostructure attached to a peptide sequence, the peptide sequence includes a binding sequence with an affinity toward EGFR, a ligand bound to gold atoms of the nanorod, a positively charged amino acid that maintains activity of the binding sequence, and a unit that increases hydrophilicity of the peptide sequence.

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07-02-2019 дата публикации

COMPOSITIONS AND METHODS FOR ENTRAPPING PROTEIN ON A SURFACE

Номер: US20190039041A1
Автор: Hogan Michael E.
Принадлежит: GENOMICS USA, INC.

The present invention provides a formulation to link protein to a solid support that comprises one or more proteins, Oligo-dT and one or more non-volatile, water-soluble protein solvents, solutes or combination thereof in an aqueous solution. Further provided is a method of attaching a protein to a surface of a substrate. The formulations provided herein are contacted onto the substrate surface, printed thereon and air dried. The substrate surface is irradiated with UV light to induce thymidine photochemical crosslinking via the thymidine moieties of the Oligo-dT. 1. A formulation to link protein to a solid support , comprising:one or more proteins;Oligo-dT; andone or more non-volatile, water-soluble protein solvents, solutes or combination thereof in an aqueous solution.wherein the water-soluble protein solvent comprises propanediol or the water-soluble protein solvent and solids comprise propanediol and at least one of sucrose, trehalose or sorbitol.2. The formulation of claim 1 , wherein said sucrose claim 1 , trehalose or sorbitol is present at a mass ratio of about 0.5:1 up to about 4:1 relative to propanediol.3. The formulation of claim 1 , wherein the water soluble protein solvents and solids comprise glycerol and propanediol and at least one of sucrose claim 1 , trehalose or sorbitol.4. The formulation of claim 1 , wherein the solid support is an amino-silane layer disposed upon an underlying surface.5. The formulation of claim 4 , wherein said underlying surface is a metal surface claim 4 , a glass surface or a ceramic surface. This application is a divisional application of U.S. application Ser. No. 15/668,169, filed Aug. 3, 2017, now allowed; which is a divisional application of U.S. application Ser. No. 14/120,278, filed May 14, 2014, now U.S. Pat. No. 9,751,069, issued Sept. 5, 2017; which claims benefit of priority under 35 U.S.C. § 119(e) of provisional application U.S. Ser. No. 61/823,065, filed May 14, 2013, the entirety of which are hereby ...

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16-02-2017 дата публикации

BIOCHEMISTRY REACTIVE MATERIAL AND DEVICE FOR ELIMINATING ELECTRONEGATIVE LOW-DENSITY LIPOPROTEIN (LDL) AND METHOD FOR TREATING BLOOD OR PLASMA EX VIVO TO ELIMINATE ELECTRONEGATIVE LOW-DENSITY LIPOPROTEIN THEREIN

Номер: US20170044516A1

The present disclosure provides a biochemistry reactive material, including a substrate and an enzyme composition immobilized on the substrate. The enzyme composition is selected from a group consisting of a first enzyme, a second enzyme, and a combination thereof. The first enzyme is used for eliminating a glycan residue of an electronegative low-density lipoprotein (electronegative LDL). The second enzyme is used for eliminating ceramide carried by an electronegative low-density lipoprotein. The biochemistry reactive material is capable of eliminating electronegative low-density lipoprotein. 1. A biochemistry reactive material , comprising:a substrate; and a first enzyme for eliminating a glycan residue of an electronegative low-density lipoprotein (electronegative LDL);', 'a second enzyme for eliminating ceramide carried by an electronegative low-density lipoprotein; and', 'a combination thereof,, 'an enzyme composition immobilized on the substrate, wherein the enzyme composition is selected from a group consisting ofwherein the biochemistry reactive material is capable of eliminating electronegative low-density lipoprotein.2. The biochemistry reactive material as claimed in claim 1 , wherein the substrate comprises silica gel claim 1 , cellulose claim 1 , diethylaminoethyl cellulose (DEAE cellulose) claim 1 , chitosan claim 1 , polystyrene claim 1 , polysulfone claim 1 , polyethersulfone claim 1 , acrylate resin or polysaccharide.3. The biochemistry reactive material as claimed in claim 1 , wherein the substrate has a particle structure or a hollow-tube structure.4. The biochemistry reactive material as claimed in claim 1 , wherein the substrate is a cellulose bead.5. The biochemistry reactive material as claimed in claim 1 , wherein the substrate is a chitosan bead.6. The biochemistry reactive material as claimed in claim 1 , wherein the substrate is a cellulose hollow fiber claim 1 , a polysulfone hollow fiber claim 1 , epoxy acrylic resin or a ...

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15-02-2018 дата публикации

METHOD OF MANUFACTURING PROTEIN ARRAY OR PEPTIDE ARRAY, METHOD OF IDENTIFYING FUNCTIONAL PROTEIN OR FUNCTIONAL PEPTIDE, PROTEIN ARRAY OR PEPTIDE ARRAY, AND FUNCTIONAL PROTEIN OR FUNCTIONAL PEPTIDE IDENTIFICATION KIT

Номер: US20180044665A1
Принадлежит:

There is provided a method of manufacturing a protein array or peptide array suitable for an efficient screening of a functional protein or functional peptide. The method of manufacturing a protein array or peptide array includes the steps of: (a) preparing a nucleic acid immobilized on a solid support and a cell-free synthesis system in a reactor, in which a reactor array includes the reactor having a specific aperture shape and a protein capture molecule or a peptide capture molecule provided on at least a portion of wall surface and bottom surface in the reactor; and (c) synthesizing a protein or peptide from the nucleic acid using the cell-free synthesis system and immobilizing the protein or peptide in the reactor. 115-. (canceled)16. A method of screening a functional protein or a functional peptide , comprising:(a) disposing a nucleic acid immobilized on a solid support and a cell-free synthesis system in a reactor, in which a reactor array includes the reactor having a specific aperture shape and a protein capture molecule or a peptide capture molecule provided on at least a portion of wall surface and bottom surface in the reactor; and(c) manufacturing a protein array or a peptide array by synthesizing a protein or a peptide from the nucleic acid using the cell-free synthesis system and immobilizing the protein or the peptide in the reactor(d) performing a functional screening using the protein array or the peptide array to specify a reactor containing a functional protein or a functional peptide.17. The method of screening a functional protein or a functional peptide according to claim 16 , further comprising:(e) recovering, before (d), at least one nucleic acid in the reactor.18. The method of screening a functional protein or a functional peptide according to claim 17 ,wherein the (e) is superimposing a substrate having an affinity to the solid support with the reactor array, thereby printing the nucleic acid on the substrate.19. A method of screening a ...

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14-02-2019 дата публикации

Blood Treatment With Inactivation Of Circulating Nucleic Acids

Номер: US20190046717A1
Принадлежит: FRESENIUS MEDICAL CARE DEUTSCHLAND GMBH

The present invention relates to a device for the treatment of blood comprising a solid phase on which a polypeptide is immobilized which is suitable for the inactivation of free nucleic acids. Suitable polypeptides are, for example, deoxyribonucleases, ribonucleases, DNA methyltransferases or cytosine deaminases. The invention further comprises the use of such devices for the treatment of patients suffering from chronic kidney failure, cancer or lupus erythematosus, as well as methods and systems for the treatment of blood, wherein free nucleic acids are inactivated outside the body. 1. A device for the treatment of blood , comprising(a) tubes for whole blood or blood plasma to flow through from and to the patient,(b) a solid phase on which a polypeptide is immobilized which is suitable for the inactivation of free nucleic acids.2. The device according to claim 1 , wherein the device furthermore comprises (c) a dialyzer or haemofilter.3. The device according to claim 1 , wherein the polypeptide is selected from the group consisting of deoxyribonucleases claim 1 , ribonucleases claim 1 , endonucleases claim 1 , exonucleases claim 1 , endoribonucleases claim 1 , exoribonucleases or peptides with nuclease activity.4. The device according to claim 1 , wherein the polypeptide is selected from the group consisting of DNA methyltransferases 1 (DNMT1) or peptides with methyltransferase activity.5. The device according to claim 1 , wherein the polypeptide has a cytosine deaminase activity.6. The device according to claim 2 , wherein the solid phase is upstream of the dialyzer or haemofilter.7. The device according to claim 2 , wherein the solid phase is located within the dialyzer or haemofilter.8. The device according to claim 1 , wherein the device furthermore comprises (d) a plasma filter.9. The device according to claim 1 , wherein the solid phase on which the polypeptide is immobilized comprises a hollow fibre membrane claim 1 , beads or a non-woven.10. The device ...

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25-02-2021 дата публикации

AFFINITY LIGANDS FOR ANTIBODY FC REGION

Номер: US20210054042A1
Принадлежит:

The present invention relates to ligand that may be a peptide compound as well as peptoid or retro-inverso analogues thereof with binding affinity for the Fc region of immunoglobulins. The invention further relates to the application of such peptides and variants thereof for purification of immunoglobulins on the basis of affinity chromatography, non-covalent antibody labelling, antibody detection or immobilization of antibodies to solid support. 142.-. (canceled)44. The ligand of claim 43 , wherein Xis not present.45. The ligand of claim 43 , wherein Xis present.46. The ligand of claim 45 , wherein Xis G.47. The ligand of claim 43 , wherein Xis not present.48. The ligand of claim 43 , wherein Xis present.49. The ligand of claim 48 , wherein Xis S claim 48 , T claim 48 , C claim 48 , N or K.50. The ligand of claim 43 , wherein Xis Y claim 43 , W or F.51. The ligand of claim 43 , wherein Xis W claim 43 , Y or F.52. The ligand of claim 43 , wherein Xis Y claim 43 , W or F.53. The ligand of claim 43 , wherein Xis A claim 43 , D claim 43 , E claim 43 , N claim 43 , Q or K.54. The ligand of claim 43 , wherein Xis V claim 43 , A claim 43 , K claim 43 , C claim 43 , I claim 43 , L or M.55. The ligand of claim 43 , wherein Xis W claim 43 , Y or F.56. The ligand of claim 43 , wherein Xis F claim 43 , W or Y.57. The ligand of claim 43 , wherein the ligand comprises an amino acid sequence having at least 60% claim 43 , such as at least 70% claim 43 , sequence identity with any one of the amino acid sequences SEQ ID NO: 2 to SEQ ID NO: 173.58. The ligand of claim 43 , wherein the ligand consists of any one of the amino acid sequences SEQ ID NO: 2 to SEQ ID NO: 173.59. A retro-inverso analogue or peptidomimetic of the ligand of .60. A solid phase support claim 43 , on which the ligand of is immobilized.61. A method for purifying immunoglobulins or Fc region-containing proteins thereof in a sample claim 43 , comprising the steps a) to c):{'claim-ref': {'@idref': 'CLM-00043', ' ...

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26-02-2015 дата публикации

SURFACE-BOUND FLUORINATED ESTERS FOR AMINE CAPTURE

Номер: US20150057438A1
Принадлежит:

A method for immobilizing an amino-containing material to a substrate is described. The method involves providing a tethering compound with two reactive groups: a substrate reactive group and a fluoroalkoxycarbonyl group. The method further involves preparing a substrate-attached tethering group by reacting the substrate reactive group of the tethering compound with a complementary functional group on the surface of a substrate. The substrate-attached tethering group has a fluoroalkoxycarbonyl group that can be reacted with an amino-containing material to form an immobilization group that connects the amino-containing material to the substrate. 2. The article of claim 1 , wherein T is the remainder of biological amino-containing material.3. The article of claim 2 , wherein T is further associated with a second biological material.4. The article of claim 1 , wherein Y is an alkylene or Y comprises a first alkylene connected to at least one other group selected from a heteroalkylene claim 1 , arylene claim 1 , second alkylene claim 1 , carbonyl claim 1 , carbonyloxy claim 1 , carbonylimino claim 1 , oxy claim 1 , thio claim 1 , —NR— claim 1 , or combination thereof.5. The article of claim 1 , wherein Y is a heteroalkylene or Y comprises a first heteroalkylene connected to at least one other group selected from an alkylene claim 1 , arylene claim 1 , second heteroalkylene claim 1 , carbonyl claim 1 , carbonyloxy claim 1 , carbonylimino claim 1 , oxy claim 1 , thio claim 1 , —NR— claim 1 , or combination thereof.6. The article of claim 1 , wherein Y is an arylene or Y comprises a first arylene connected to at least one other group selected from an alkylene claim 1 , heteroalkylene claim 1 , second arylene claim 1 , carbonyl claim 1 , carbonyloxy claim 1 , carbonylimino claim 1 , oxy claim 1 , thio claim 1 , —NR— claim 1 , or combination thereof. This application is a Divisional application of pending prior U.S. application Ser. No. 11/856,140, filed Sep. 17, 2007, now ...

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10-03-2022 дата публикации

SUBSTANCES AND METHODS FOR THE USE IN PREVENTION AND/OR TREATMENT IN HUNTINGON'S DISEASE

Номер: US20220073650A1
Принадлежит: Affiris AG

Disclosed is an apheresis device including a solid carrier capable of being contacted with the blood or plasma flow, characterised in that the solid carrier includes one or several HTT-binding molecule (s) capable of adsorbing HTT or fragments thereof in a specific manner from plasma or blood or other HTT containing body fluids such as CSF. 1. A method of treating Huntington's disease and/or delaying the onset of clinical symptoms of Huntington's disease , the method comprising administering to a subject in need thereof a vaccine composition comprising at least one immunogenic peptide of Huntingtin (HTT) protein , wherein the at least one immunogenic peptide is selected from the group consisting of p7564 (CPSDSSEIVLD , SEQ ID No. 2) , p7543 (GTDNQYLGLQIGC , SEQ ID No. 3) , p7543a (DNQYLGLQIC; SEQ ID No. 88) , wherein the N- or C-terminal cysteine residue (C) may be present or not or provided alternatively at the C- or N-terminus; or peptides comprising at least one of these peptides in a total length of maximally 50 amino acid residues.2. The method according to claim 1 , wherein the at least one immunogenic peptide is selected from the group consisting of p9394 (KTDNQYLGLQIGKC; SEQ ID No. 91) claim 1 , p9395 (GTDNQYLGLQIGKKC; SEQ ID No. 92) claim 1 , p9396 (KTDNQYLGLQIKKGC; SEQ ID No. 93) claim 1 , p9397 (KDNQYLGLQIKKGC; SEQ ID No. 94); p7543b (TDNQYLGLQIC; SEQ ID No. 89) claim 1 , p7543c (TDNQYLGLQIGC; SEQ ID No. 90) claim 1 , p8346 (CGPAVAEEPLHRP claim 1 , SEQ ID No. 5) claim 1 , p8855 (SDSSEIVLDGTDC claim 1 , SEQ ID No. 6) claim 1 , p8858 (EIVLDGTDNQYLC claim 1 , SEQ ID No. 7) claim 1 , p8859 (IVLDGTDNQYLGC claim 1 , SEQ ID No. 8) claim 1 , p8860 (VLDGTDNQYLGLC claim 1 , SEQ ID No. 9) claim 1 , p8861 (LDGTDNQYLGLQC claim 1 , SEQ ID No. 10) claim 1 , p8862 (DGTDNQYLJGLQIGC claim 1 , SEQ ID No. 11) claim 1 , p8869 (CTDNQYLGLQIGQ claim 1 , SEQ ID No. 12) claim 1 , p8868 (CGTDNQYLGLQIG claim 1 , SEQ ID No. 13) claim 1 , p8870 (CDNQYLGLQIGQP claim 1 , SEQ ID No. 14) ...

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05-03-2015 дата публикации

Preassembled hybrid nanocluster plasmonic resonator for immunological detection and serotyping of virus and microbes

Номер: US20150065694A1
Принадлежит: United States Department of Energy

Here, we describe a preassembled plasmonic resonance nanocluster. One embodiment is used for microbe detection and typing. The metallic nanoparticle acceptors with microbe surface antigen epitope, and quantum dot (QD) donors with Fab antibody, are assembled into an immuno-mediated 3D-oriented complex with enhanced energy transfer and fluorescence quenching. The coherent plasmonic resonance between the metal and QD nanoparticles is exploited to achieve improved donor-acceptor resonance within the nanocluster, which in the presence of microbial particles is disassembled in a highly specific manner. The nanocluster provides high detection specificity and sensitivity of the microbes, with a sensitivity limit down to 1-100 particles per microliter and to attomolar levels of a surface antigen epitope. A few specific examples of the plasmonic resonance nanocluster used in microbe detection are disclosed along with ways in which the complex can be easily modified for additional microbes. 1. A nanocluster complex for identifying the presence of one or more microbes comprising:a. a single core nanoparticle conjugate (CNC), wherein said CNC comprises a quantum dot covalently linked to one or more fragment antigen-binding (Fab) antibodies;b. one or more multiple capping nanoparticle conjugates (MCNCs), wherein each said MCNC comprises a metal nanoparticle functionalized with one or more peptide epitopes; andc. at least one linkage between said CNC and one or more said MCNCs, wherein said linkage comprises one or more peptide epitopes of said MCNCs and said Fab antibodies targeting said epitopes on said CNC.2. The complex of wherein said linkage comprises one peptide epitope and said Fab antibody targets said epitope.3. The complex of wherein:a. said single peptide epitope comprises at least 85 percent homology to the sequence of Hepatitis B Virus surface antigen preS2;b. said Fab fragments targeting said epitope are derived from monoclonal antibody against said HBV preS2 ...

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11-03-2021 дата публикации

SIDE CHAIN MODIFIED PEPTOIDS USEFUL AS STRUCTURE-STABILIZING COATINGS FOR BIOMATERIALS

Номер: US20210070886A1
Принадлежит:

The current invention pertains compositions and methods to generate compositions providing stability to biomolecules, including providing physiologically stable and functional DNA origami-based drug/gene delivery carriers by surface coating with the oligo-ethylene glycol conjugated peptoids of Formulas (I), (II), and (III). 2. The composition according to claim 1 , wherein R claim 1 , R claim 1 , R claim 1 , R claim 1 , R claim 1 , R claim 1 , R claim 1 , and Rare independently —(CH)—Calkyne claim 1 , —((CH)—O)—CH claim 1 , —((CH)—O)—CH claim 1 , or —(CH)—NH.3. The composition according to of claim 1 , wherein at least one of R-Rcomprise a positively charged group; and R-Rdo not comprise a positively charged group.4. The composition according to claim 1 , wherein R claim 1 , R claim 1 , R claim 1 , R claim 1 , R claim 1 , R claim 1 , R claim 1 , and Rare independently selected from the group consisting of —(CH)—NH claim 1 , —(CH)—NH claim 1 , —(CH)—NH claim 1 , —(CH)—NH claim 1 , —(CH)—NH claim 1 , —(CH)—NH claim 1 , —(CH)—NH claim 1 , —(CH)—Calkyne claim 1 , —((CH)—O)—CH claim 1 , —((CH)—O)—CH claim 1 , and —(C-C)alkylene-N.8. The composition according to claim 1 , wherein the compound of Formula (I) claim 1 , is conjugated to an antibody claim 1 , imaging reagent claim 1 , biomaterial claim 1 , biomolecule claim 1 , glycan claim 1 , polymer claim 1 , or a peptoid.9. A drug delivery carrier comprising a pre-defined nucleic acid nanostructure and a compound of Formula (I) claim 1 , (II) claim 1 , or (III).10. A stabilized complex comprising:a pre-defined nucleic acid nanostructure;a compound of Formula (I), (II), or (III); anda drug molecule or protein.11. The stabilized complex according to claim 10 , wherein an antibody is conjugated to the compound of Formula (I) claim 10 , (II) claim 10 , or (III).12. A method of stabilizing a pre-defined nucleic acid nanostructure claim 10 , said method comprising:(i) complexing a pre-defined nucleic acid nanostructure with a ...

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15-03-2018 дата публикации

CXCR4 BINDING MOLECULES

Номер: US20180072816A1
Принадлежит:

The present disclosure relates to polypeptides (also referred to herein as CXCR4 binding molecules or polypeptides) that are directed against the G-coupled protein receptor CXCR4, also known as Fusin or CD184. The invention also relates to nucleic acids encoding such polypeptides; to methods for preparing such polypeptide; to compositions, and in particular to pharmaceutical compositions that comprise such polypeptides and to uses of such polypeptides for therapeutic or diagnostic purposes. 141-. (canceled)42. A polypeptide which binds to human CXCR4 , comprising a scaffold region and complementarity determining regions (CDR1 and CDR3) contained therein , the scaffold region comprising a sequence which has at least 75% identity to the scaffold region defined by amino acids 1 to 26 , 33 to 79 and 88 to 97 of SEQ ID NO:1; andwherein the CDR1 and CDR3 region defined by amino acids 27 to 32 and 80-87 respectively of SEQ ID NO:1 are modified by amino acid addition or substitution therein; andwherein the CDR3 region comprises or consists of a sequence having at least 70% identity to SEQ ID NO: 13, SEQ ID NO: 16, SEQ ID NO: 19, SEQ ID NO: 22, SEQ ID NO: 25, SEQ ID NO: 28, or SEQ ID NO: 31.43. The polypeptide according to claim 42 , wherein the scaffold region comprises between 1 and 5 amino acid additions or substitutions within the sequence set forth in SEQ ID NO:2 or comprises the sequence set forth in SEQ ID NO:2.44. The polypeptide according to claim 43 , wherein the amino acid designated by A′ at position 23 of SEQ ID NO:2 is the amino acid residue glutamine (Q) or lysine (K); and the amino acid designated by B′ at position 24 of SEQ ID NO:2 is the amino acid residue valine (V) or alanine (A).45. The polypeptide according to claim 42 , which is an antagonist of human CXCR4.46. The polypeptide according to claim 42 , wherein:the CDR3 region comprises or consists of a sequence having at least one, two, three, four or five amino acid substitutions within a sequence ...

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22-03-2018 дата публикации

APOLIPOPROTEIN NANODISCS WITH TELODENDRIMER

Номер: US20180079829A1
Принадлежит:

The present invention provides a nanodisc with a membrane scaffold protein. The nanodisc includes a membrane scaffold protein, a telodendrimer and a lipid. The membrane scaffold protein can be apolipoprotein. The telodendrimer has the general formula PEG-L-D-(R), wherein D is a dendritic polymer; L is a bond or a linker linked to the focal point group of the dendritic polymer; each PEG is a polyethylene glycol) polymer; each R is and end group of the dendritic polymer, or and end group with a covalently bound hydrophobic group, hydrophilic group, amphiphilic compound, or drug; and subscript n is an integer from 2 to 20. Cell free methods of making the nanodiscs are also provided. 1. A nanodisc comprising:a membrane scaffold protein;a telodendrimer; anda lipid.2. The nanodisc of claim 1 , wherein the membrane scaffold protein is apolipoprotein.4. The nanodisc of claim 3 , wherein the dendritic polymer is a poly(lysine) dendritic polymer wherein each end group is hydroxy.5. The nanodisc of claim 3 , wherein each amphiphilic compound is cholic acid (CA).6. The nanodisc of claim 5 , wherein the telodendrimer is selected from the group consisting of PEG-D-CA claim 5 , PEG-D-CAand PEG-D-CA claim 5 , wherein each dendritic polymer D is a poly(lysine) dendritic polymer wherein each end group is hydroxy.7. The nanodisc of claim 1 , wherein the lipid is selected from the group consisting of a phospholipid claim 1 , cholesterol claim 1 , a phosphatidylcholine claim 1 , a phosphatidylethanolamine claim 1 , a phosphatidylglycerol claim 1 , a phosphatidylserine claim 1 , and a phosphatidylinositol.8. The nanodisc of claim 7 , wherein the lipid is selected from the group consisting of 1 claim 7 ,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) claim 7 , 1 claim 7 ,2-ditetradecanoyl-sn-glycero-3-phosphocholine (DMPC) claim 7 , 1-tetradecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine (WPC) claim 7 , 1 claim 7 ,2-dioctadecanoyl-sn-glycero-3-phosphocholine (DSPC) claim 7 , ...

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25-03-2021 дата публикации

CAPTURE, PURIFICATION, AND RELEASE OF BIOLOGICAL SUBSTANCES USING A SURFACE COATING

Номер: US20210088514A1
Принадлежит:

This invention relates to a surface coating for capture circulating rare cells, comprising a nonfouling composition to prevent the binding of non-specific cells and adsorption of serum components; a bioactive composition for binding the biological substance, such as circulating tumor cells; with or without a linker composition that binds the nonfouling and bioactive compositions. The invention also provide a surface coating for capture and purification of a biological substance, comprising a releasable composition to release the non-specific cells and other serum components; a bioactive composition for binding the biological substance, such as circulating tumor cells; with or without a linker composition that binds the releasable and bioactive compositions. The present invention also discloses a novel microfluidic chip, with specific patterned microstructures to create a flow disturbance and increase the capture rate of the biological substance. 163.-. (canceled)64. A microfluidic chip for selectively enriching rare cells , comprising:a first solid substrate and a second solid substrate, wherein at least one of the first and second solid substrates comprise a series of microstructures configured to interact with cells, wherein the series of microstructures are perpendicular to a flow direction of the microfluidic chip, and wherein the first and second solid substrates are configured to be bound parallel to one another; anda surface coating for capturing the rare cells, wherein the surface coating comprises a non-fouling composition and a bioactive composition which selectively binds to the rare cells, wherein the non-fouling composition of the surface coating is non-covalently associated with the bioactive composition,wherein at least one of the first and second solid substrates comprise the surface coating.65. The microfluidic chip of claim 64 , wherein the microstructures are arranged in a linear pattern such that microstructures in a first pair of adjacent rows ...

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31-03-2016 дата публикации

METHOD FOR THE DETECTION, PREPARATION AND DEPLETION OF CD4+ T LYMPHOCYTES

Номер: US20160091492A1
Принадлежит:

The present invention relates an in vitro method for detecting class II restricted CD4+ T cells in a sample. Herein a sample is contacted with an isolated complex of an MHC class II molecule and a peptide. This peptide comprises an MHC class II restricted T cell epitope of an antigenic protein and immediately adjacent thereof, or separated by a linker of at most 7 amino acids a sequence with a [CST]-xx-C or C-xx-[CST] motif. CD4+ T cells are detected by measuring the binding of the complex with cells in the sample, wherein the binding of the complex to a cell is indicative for the presence of CD4+ T cells in the sample. The present invention further relates to an isolated complex of an MHC Class II molecule and a peptide comprising an MHC class II restricted T cell epitope of an antigenic protein and immediately adjacent thereof, or separated by a linker of at most 7 amino acids a sequence with a [CST]-xx-C or C-xx-[CST] motif. 130-. (canceled)31. An in vitro method for detecting class II restricted CD4+ T cells in a sample comprising the steps of:providing a sample,contacting the sample with a complex of an isolated MHC class II molecule and a peptide, said peptide comprising an MHC class II restricted T cell epitope of an antigenic protein and immediately adjacent thereof, or separated by a linker of at most 7 amino acids, a sequence with a [CST]-X(2)-C or C—X(2)-[CST] redox motif, wherein X is any amino acid,measuring the binding of said complex with cells in said sample, wherein the binding of said complex to a cell is indicative for the presence of CD4+ T cells in said sample.32. The method according to claim 31 , wherein said redox motif is C—X(2)-C.33. The method according to claim 31 , wherein said linker has a length of maximum 4 amino acids.34. The method according to claim 31 , wherein said peptide occurs in a non-covalent complex with the MHC class II molecule and has a length of between 12 and 20 amino acids.35. The method according to claim 31 , ...

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05-05-2022 дата публикации

METHOD FOR SUPPORTING THIOL GROUP-INCLUDING COMPOUND

Номер: US20220135705A1
Принадлежит: KANEKA CORPORATION

The objective of the present invention is to provide a method for efficiently supporting a thiol group-including compound on an insoluble base material. The method for supporting a thiol group-including compound on an insoluble base material according to the present invention is characterized in comprising Step A: treating the thiol group-including compound with a thiol group-including organic reducing agent and an inorganic reducing agent, and Step B: contacting a reaction liquid of said Step A with the insoluble base material.

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14-04-2016 дата публикации

USE OF METAL COMPLEXES

Номер: US20160103126A1
Принадлежит: ANTEO TECHNOLOGIES PTY LTD

A method of immobilising a target molecule on a substrate, which comprises exposing the target molecule to the substrate in the presence of a metal complex, wherein the target molecule is an unmodified target molecule, and wherein the metal complex is selected to provide a stable binding interaction between the target molecule and the substrate. 2. The substrate of claim 1 , wherein said compound is selected from the group consisting of perchlorate claim 1 , chloride claim 1 , acetate claim 1 , bromide claim 1 , nitrate claim 1 , perchlorate claim 1 , alum claim 1 , sulphate claim 1 , and hydroxide.3. The substrate of claim 1 , wherein said transition metal ion is selected from the group consisting of rhodium claim 1 , platinum claim 1 , scandium claim 1 , titanium claim 1 , vanadium claim 1 , chromium claim 1 , ruthenium claim 1 , manganese claim 1 , iron claim 1 , cobalt claim 1 , nickel claim 1 , copper claim 1 , molybdenum claim 1 , zirconium and zinc.4. The substrate of claim 1 , wherein said substrate takes the form of a bead claim 1 , membrane claim 1 , multi-well plate claim 1 , slide claim 1 , or capillary column.5. The substrate of claim 1 , wherein said substrate is a carboxylic acid functionalised claim 1 , amide functionalised claim 1 , amine functionalised or ester functionalised substrate.6. The substrate of claim 1 , wherein said target molecule is a protein.7. The substrate of claim 6 , wherein said protein is an antibody. The present application is a divisional of U.S. application Ser. No. 11/571,422, filed Jan. 14, 2008, which is a 371 of International Application No. PCT/AU2005/000966, filed Jun. 30, 2005, and claims priority from U.S. Provisional Application Nos. 60/585,261, filed Jul. 2, 2004, and 60/645,053, filed Jan. 18, 2005, each of which is hereby incorporated by reference in its entirety.The present invention relates to a method for immobilising a target molecule on a substrate via metal complexes, to the use of a metal complex in this ...

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12-04-2018 дата публикации

RATIONALLY-DESIGNED SYNTHETIC PEPTIDE SHUTTLE AGENTS FOR DELIVERING POLYPEPTIDE CARGOS FROM AN EXTRACELLULAR SPACE TO THE CYTOSOL AND/OR NUCLEUS OF A TARGET EUKARYOTIC CELL, USES THEREOF, METHODS AND KITS RELATING TO SAME

Номер: US20180100158A1
Принадлежит:

The present description relates to methods for delivering polypeptide cargos from an extracellular space to the cytosol and/or nucleus of a target eukaryotic cell. The methods involve contacting the cell with the polypeptide cargo in the presence of a peptide shuttle agent at a concentration sufficient to increase the polypeptide cargo's transduction efficiency. Also described here are parameters that may be used in the rational design of such synthetic peptide shuttle agents, peptide shuttle agents that satisfy one or more of these design parameters, as well as methods and compositions relating to the use of the synthetic peptide shuttle agents for delivery of a variety of polypeptide cargos (such as transcription factors, antibodies, CRISPR-associated nucleases and functional genome editing complexes) from an extracellular space to the cytosol and/or nucleus of target eukaryotic cells. Applications and targets for genome-editing NK cells for improved immunotherapy are also described. 2. The method of claim 1 , wherein the shuttle agent respects at least six claim 1 , at least seven claim 1 , at least eight claim 1 , at least nine claim 1 , at least ten claim 1 , at least eleven claim 1 , or all of parameters (4) to (15).3. The method of claim 1 , wherein said shuttle agent comprises a hydrophobic moment (μ) between a lower limit of 4.0 claim 1 , 4.1 claim 1 , 4.2 claim 1 , 4.3 claim 1 , 4.4 claim 1 , 4.5 claim 1 , 4.6 claim 1 , 4.7 claim 1 , 4.8 claim 1 , 4.9 claim 1 , 5.0 claim 1 , 5.1 claim 1 , 5.2 claim 1 , 5.3 claim 1 , 5.4 claim 1 , 5.5 claim 1 , 5.6 claim 1 , 5.7 claim 1 , 5.8 claim 1 , 5.9 claim 1 , 6.0 claim 1 , 6.1 claim 1 , 6.2 claim 1 , 6.3 claim 1 , 6.4 claim 1 , 6.5 claim 1 , 6.6 claim 1 , 6.7 claim 1 , 6.8 claim 1 , 6.9 claim 1 , 7.0 claim 1 , and an upper limit of 9.5 claim 1 , 9.6 claim 1 , 9.7 claim 1 , 9.8 claim 1 , 9.9 claim 1 , 10.0 claim 1 , 10.1 claim 1 , 10.2 claim 1 , 10.3 claim 1 , 10.4 claim 1 , or 10.5.5. The method of claim 4 , wherein ...

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13-04-2017 дата публикации

METHOD FOR PHOTO-IMMOBILIZING BIOMOLECULES ON A NON-FUNCTIONALIZED CARRIER

Номер: US20170102380A1
Принадлежит:

The immobilization of biomolecules on a non-functionalized carrier by irradiating the biomolecule-impregnated carrier with a light of a wavelength of at least 340 nm. 115-. (canceled)16. A process for immobilizing biomolecules on a non-functionalized carrier comprising the steps of:(i) impregnating the non-functionalized carrier with a solution containing the said biomolecules; and(ii) irradiating the impregnated carrier resulting from step (i) with a light of a wavelength of at least 340 nm;wherein said biomolecules are not functionalized;wherein the non-functionalized carrier is selected from cellulose, or the non-functionalized carrier is selected from polyethylene terephthalate (PET), polyethylene naphthalate (PEN), poly(methyl methacrylate) (PMMA), polyurethane (PU), poly(vinyl chloride) (PVC), polyethylene (PE), polystyrene (PS), polylactate, polyamide, and combinations thereof;wherein the process further comprises a preliminary step, before step (i), of rendering the said non-functionalized carrier substantially non-porous, comprising the steps of:a) impregnating said non-functionalized carrier with at least one filler until saturation of the carrier, andb) drying the impregnated non-functionalized carrier resulting from step a).17. The process according to claim 16 , further comprising a step of drying said impregnated carrier after step (i) and before step (ii).18. The process according to claim 16 , further comprising at least one step of washing the irradiated carrier resulting from step (ii).19. The process according to claim 16 , wherein the light used for irradiating the impregnated carrier has a wavelength of from 340 nm to 800 nm.20. The process according to claim 16 , wherein said impregnated carrier is irradiated during step (ii) with a photoenergy of from 1 mJ/cmto 500 J/cm.21. The process according to claim 16 , wherein said non-functionalized carrier is substantially non-porous.22. The process according to claim 16 , wherein said non- ...

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19-04-2018 дата публикации

PEPTIDES, DEVICES, AND METHODS FOR THE DETECTION OF EHRLICHIA ANTIBODIES

Номер: US20180106792A1
Принадлежит:

The invention provides peptide compositions and mixtures useful for the detection of antibodies that bind to antigens. The peptide compositions and mixtures comprise polypeptide sequences based on an immunogenic fragment of the Outer Membrane Protein 1 (OMP-1) protein. The invention also provides devices, methods, and kits comprising such peptide compositions and mixtures useful for the detection of antibodies that bind to antigens and the diagnosis of monocytic and/or granulocytic ehrlichiosis. 1. A population of isolated peptides comprising three or more different peptides , wherein each peptide in the population comprises a sequence of:{'sub': 2', '5', '8', '10', '11', '12', '13', '18', '20', '22', '23', '24', '25', '26', '39', '44', '49', '56', '58, '(i) S-X-K-E-X-K-Q-X-T-X-X-X-X-G-L-K-Q-X-W-X-G-X-X-X-X-X-G-G-G-G-G-N-F-S-A-K-E-E-X-A-E-T-R-X-T-F-G-L-X-K-Q-Y-D-G-A-XI-X-E-N-Q-V-Q-N-K-F-T-I-S-N-C (SEQ ID NO: 72) or fragment thereof,'}{'sub': 5', '8', '10', '11', '12', '13', '18', '20', '22', '23', '24', '25', '26', '39', '44', '49', '56', '58, 'wherein X2 is an amino acid selected from the group consisting of A and V, Xis an amino acid selected from the group consisting of E and D, Xis an amino acid selected from the group consisting of T and P, Xis an amino acid selected from the group consisting of T and V, Xis an amino acid selected from the group consisting of G and A, Xis an amino acid selected from the group consisting of L and V, Xis an amino acid selected from the group consisting of Y and F, Xis an amino acid selected from the group consisting of D and N, Xis an amino acid selected from the group consisting of D and N, Xis an amino acid selected from the group consisting of S and V, Xis an amino acid selected from the group consisting of A, S, and T, Xis an amino acid selected from the group consisting of A and I, Xis an amino acid selected from the group consisting of T and P, Xis an amino acid selected from the group consisting of S, N, and K, Xis any ...

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03-05-2018 дата публикации

TIM PROTEIN-BOUND CARRIER, METHODS FOR OBTAINING, REMOVING AND DETECTING EXTRACELLULAR MEMBRANE VESICLES AND VIRUSES USING SAID CARRIER, AND KIT INCLUDING SAID CARRIER

Номер: US20180120299A1
Принадлежит:

The invention provides a carrier and a method for obtaining, removing, or detecting extracellular membrane vesicle or virus present in a sample. In particular, the invention provides (a) a carrier (a Tim carrier) on which a protein (a Tim protein), selected from a T-cell immunoglobulin and mucin domain-containing molecule-4 (a Tim-4) protein, a Tim-3 protein, and a Tim-1 protein, is bound; (b) a method for obtaining the extracellular membrane vesicle or the virus in the sample; (c) a method for removing the extracellular membrane vesicle or the virus in the sample; (d) a method for detecting the extracellular membrane vesicle or the virus in the sample; (e) a kit for capturing the extracellular membrane vesicle or the virus, comprising the Tim carrier; and f) a kit for capturing the extracellular membrane vesicle or the virus, comprising a reagent containing the Tim protein and a reagent containing the carrier. 1. A carrier (a Tim carrier) on which a protein (a Tim protein) , selected from a T-cell immunoglobulin and mucin domain-containing molecule-4 (a Tim-4) protein , a T-cell immunoglobulin and mucin domain-containing molecule-3 (a Tim-3) protein , and a T-cell immunoglobulin and mucin domain-containing molecule-1 (a Tim-1) protein , is bound.2. The Tim carrier according to claim 1 , which is for capturing an extracellular membrane vesicle or a virus.3. The Tim carrier according to claim 1 , wherein the Tim protein comprises an IgV domain.4. A method for obtaining an extracellular membrane vesicle or a virus in a sample claim 1 , comprising the following steps:(1) a step for forming a complex of a Tim protein bound to a carrier, and the extracellular membrane vesicle or the virus in a sample, in the presence of a calcium ion (complex formation step),(2) a step for separating the complex and the sample (complex separation step),(3) a step for separating the extracellular membrane vesicle or the virus from the complex to obtain the extracellular membrane vesicle ...

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24-07-2014 дата публикации

VACCINES AGAINST INFLUENZA VIRUS

Номер: US20140205622A1

Disclosed are immunogenic conjugates having the general formula: 1. A method of treating and/or inhibiting an influenza infection in a subject , comprising:selecting a subject for treatment that has, or is at risk for developing, an influenza infection; andadministering to a subject a therapeutically effective amount of an immunogenic conjugate comprising an influenza M2 ectodomain (M2e) peptide covalently linked to a carrier by a thioether linkage between a lysine amino acid residue present in carrier and a cysteine amino acid residue introduced at the C-terminal end of the M2e peptide, thereby treating and/or inhibiting the influenza infection in a subject.2. A method of producing an influenza vaccine specific for an identified influenza strain , the method comprising ,obtaining a nucleic acid sequence of the identified influenza strain encoding a hemagglutinin (HA) from the identified influenza strain;producing a nucleic acid molecule encoding an immunogenic fragment of the HA, wherein the nucleic acid molecule produced encodes the polybasic cleavage site, and wherein the nucleic acid molecule produced does not encode a leader sequence at the N-terminal end of the HA or a transmembrane domain at the C-terminal end of immunogenic fragment of the HA;expressing the immunogenic fragment of the HA in a bacterial expression system; andpurifying the expressed immunogenic fragment of the HA, thereby producing an influenza vaccine specific for an identified influenza strain.3. The method of claim 2 , further comprising adsorbing the purified immunogenic fragment of the influenza HA protein onto alum.4. The method of claim 2 , further comprising treating the immunogenic fragment of the influenza HA protein with a fixative.5. The method of claim 4 , wherein the fixative comprises formalin.6. The method of claim 2 , further comprising adding a pharmaceutically acceptable carrier to the purified immunogenic fragment of the influenza HA protein.7E. coli. The method of claim 2 ...

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23-04-2020 дата публикации

FUNCTIONALIZED WELL PLATE, METHODS OF PREPARATION AND USE THEREOF

Номер: US20200123491A1
Принадлежит:

In biosciences and related fields, it can be useful to modify surfaces of apparatuses, devices, and materials that contact biomaterials such as biomolecules and biological micro-objects. Described herein are surface modifying and surface functionalizing reagents, preparation thereof, and methods for modifying surfaces of wells within a well plate to activate lymphocytes, including but not limited to T lymphocytes, in a controllable and reproducible manner 1. A well plate comprising a surface having a first region which is a reactive moiety-presenting covalently functionalized region or an activating moiety-presenting covalently functionalized region , wherein the reactive moiety is an azido moiety , a biotin moiety or a streptavidin moiety and the activating moiety is a lymphocyte-activating moiety.2. The well plate of claim 1 , wherein the first region has an area of 0.5 mmto 50 mm.3. (canceled)4. The well plate of claim 1 , wherein the first region is substantially circular and has a diameter of 0.5 mm to 4.0 mm.5. The well plate of claim 1 , wherein the surface of the well plate further comprises a second region which is a covalently modified region comprising surface blocking ligands claim 1 , wherein the second region surrounds the first region.6. The well plate of claim 1 , wherein the surface of the well plate comprises glass or polystyrene.7. (canceled)8. The well plate of claim 1 , wherein the first region has a density of respective reactive moieties or activating moieties of at least 50/um.9. The well plate of claim 1 , wherein the first region comprises respective reactive moieties or activating moieties linked covalently to the surface via a linker having from 5 to 20 backbone atoms claim 1 , 10 to 40 backbone atoms claim 1 , or 15 to 50 backbone atoms selected from carbon claim 1 , silicon claim 1 , nitrogen and oxygen.10. The well plate of claim 1 , wherein the reactive moiety is streptavidin claim 1 , and the streptavidin functionality is covalently ...

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04-06-2015 дата публикации

CARRIER FOR ANTIBODY PURIFICATION, MANUFACTURING METHOD FOR SAME, AND APPLICATION FOR SAME

Номер: US20150152195A1
Принадлежит: DAISO CO., LTD.

An object of the present invention is to provide a carrier on which Protein A has been immobilized, the Protein A having a specific amino acid sequence that permits the desorption of antibodies under mild pH conditions (specifically, pH4.0 to 5.5) in which many antibodies do not undergo acid modification; and a manufacturing method for the carrier. An immobilization carrier (excluding an immobilization carrier having a monolith structure) on which a protein is adsorbed by electrostatic interaction, the protein consisting of an amino acid sequence represented by the general formula: R1-R2-R3-R4-R5-R6, wherein the part represented by R1-R2-R3 is used for immobilization on the immobilization carrier, wherein: the sequence represents a sequence from the amino-terminal side towards the carboxyl-terminal side; the sequence of the R2 part is the sequence of a Protein A mutant as a protein to be immobilized or a sequence in which 1 to 3 units of the sequence thereof were linked together, the Protein A mutant having characteristics of strongly binding to an antibody under neutral conditions and dissociating with the antibody bound under neutral conditions under weakly acidic conditions of pH 4.0 to 5.5. 1. An immobilization carrier , excluding an immobilization carrier having a monolith structure , on which a protein is adsorbed by electrostatic interaction , the protein consisting of an amino acid sequence represented by the general formula: R1-R2-R3-R4-R5-R6 , wherein the part represented by R1-R2-R3 is used for immobilization on the immobilization carrier , wherein:the sequence represents a sequence from the amino-terminal side towards the carboxyl-terminal side;the sequence of the R1 part may be absent, and, if present, is a sequence composed of amino acid residues other than lysine and cysteine residues;the sequence of the R2 part is the sequence of a Protein A mutant as a protein to be immobilized or a sequence in which 1 to 3 units of the sequence thereof were linked ...

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25-05-2017 дата публикации

SUBSTANCES AND METHODS FOR THE USE IN PREVENTION AND/OR TREATMENT IN HUNTINGTON'S DISEASE

Номер: US20170145117A1
Автор: BARTL Stefan, SMRZKA Oskar
Принадлежит: Affiris AG

Disclosed is an apheresis device comprising a solid carrier capable of being contacted with the blood or plasma flow, characterised in that the solid carrier includes one or several HTT-binding molecule (s) capable of adsorbing HTT or fragments thereof in a specific manner from plasma or blood or other HTT containing body fluids such as CSF. 1. An apheresis device , comprising a solid carrier capable of being contacted with the blood or plasma flow , wherein the solid carrier includes a huntingtin (HTT)-binding molecule.2. The apheresis device according to claim 1 , wherein the HTT-binding molecule is an anti-HTT antibody.3. The apheresis device according to claim 1 , wherein the HTT-binding molecule is a monoclonal antibody or an HTT-binding fragment thereof.4. The apheresis device according to claim 3 , wherein the HTT-binding fragment is selected from the group consisting of a Fab fragment claim 3 , a Fd fragment claim 3 , a Fab′ fragment claim 3 , a F(ab′)2 fragment claim 3 , a Fv fragment claim 3 , and ScFv fragment.5. The apheresis device according to claim 2 , wherein the antibody is a polyclonal antibody.6. The apheresis device according to claim 2 , wherein the antibody is specific for the PRR region of HTT claim 2 , the C6 region of HTT claim 2 , or both.7. The apheresis device according to claim 1 , wherein the antibody is a monoclonal antibody selected from the group consisting of a human monoclonal antibody claim 1 , a humanized monoclonal antibody claim 1 , a bi-specific monoclonal antibody claim 1 , and a chimeric monoclonal antibody.8. The apheresis device according to claim 2 , wherein the antibody is a monoclonal antibody claim 2 , which comprises a heavy chain variable region CDR1 comprising GYSFTDFY (SEQ ID No. 54) claim 2 , a heavy chain variable region CDR2 comprising IDPKNGDT (SEQ ID No. 55) claim 2 , a heavy chain variable region CDR3 comprising ATYYGYTMDY (SEQ ID No. 56) claim 2 , a light chain variable region CDR1 comprising SSVTSSY (SEQ ID ...

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07-05-2020 дата публикации

NEW REAGENTS FOR OPTICAL MICROSCOPY

Номер: US20200141869A1
Принадлежит: Alda S.r.l.

An antibody or Fab fragment, wherein at least one amino group of the N-terminal amino acid of the light chain and/or of the N-terminal amino acid of the heavy chain is bound by an amidic bond to a molecule comprising a fluorophore group A, wherein said bond constitutes at least 70% of the total binding of said molecule to said antibody or Fab. 1) Antibody or Fab fragment , wherein at least one amino group of the N-terminal amino acid of the light chain and/or of the N-terminal amino acid of the heavy chain is bound by an amidic bond to a molecule comprising a fluorophore group A , wherein said bond constitutes at least 70% of the total binding of said molecule to said antibody or Fab , preferably at least 80% , 85% , 90% , or 98% of the total bond of said molecule to said antibody or Fab.2) Antibody or Fab fragment according to claim 1 , wherein said antibody is monoclonal or said Fab derives from a monoclonal antibody.4) Antibody or Fab fragment according to claim 3 , wherein the Z group has a total number of hydrogen-binding acceptors atoms (Num_H_Acceptors) of the molecule between 8 and 16 claim 3 , preferably between 10 and 15.5) Antibody or Fab fragment according to claim 3 , wherein the Z group has a logarithm of the water/octanol partition coefficient (A log P) between 3 and −5.6) Antibody or Fab fragment according to claim 3 , wherein the Z group has a surface accessible to the solvent (3DpolarSASA claim 3 , solvent accessible surface area) of 180 Åor more claim 3 , preferably between 200 and 550 Åand/or total polar surface (TPSA claim 3 , total polar surface area) of 180 Åor more claim 3 , preferably between 180 Åand 500 Å claim 3 , more preferably between 190 Åand 300 Å.7) Antibody or Fab fragment according to claim 3 , wherein the Z group has:Kier flexibility index ((Φ), KierFlex) between 7.5 and 15, preferably between 10 and 12,water/octanol partition coefficient logarithm (A log P) amounting to 0 or less, preferably between 0 and −10{'sup': 2', '2', '2, ...

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14-05-2020 дата публикации

COMPOSITIONS AND METHODS FOR ENTRAPPING PROTEIN ON A SURFACE

Номер: US20200147580A1
Автор: Hogan Michael E.
Принадлежит:

The present invention provides a formulation to link protein to a solid support that comprises one or more proteins, Oligo-dT and one or more non-volatile, water-soluble protein solvents, solutes or combination thereof in an aqueous solution. Further provided is a method of attaching a protein to a surface of a substrate. The formulations provided herein are contacted onto the substrate surface, printed thereon and air dried. The substrate surface is irradiated with UV light to induce thymidine photochemical crosslinking via the thymidine moieties of the Oligo-dT. 1. A composition for measuring binding to HLA proteins , comprising:a substrate having a surface; anda first array of HLA protein spots indirectly attached to the surface of the substrate, wherein each HLA protein within each spot is entrapped within a matrix that retains the native three dimensional structure of the HLA protein while the HLA protein is indirectly attached to the surface.2. The composition of claim 1 , wherein the matrix that retains the native three dimensional structure of the HLA protein comprises a cross-linked Oligo-dT network bound to the surface of the substrate.3. The composition of claim 2 , wherein each Oligo-dT in the network comprises 30-100 nucleotides.4. The composition of claim 1 , wherein the first array of HLA protein spots comprises glycerol claim 1 , propanediol claim 1 , sorbitol or trehalose.5. The composition of claim 4 , wherein the first array of HLA protein spots comprises glycerol claim 4 , propanediol claim 4 , sorbitol or trehalose in a concentration of 0.5% to 1%.6. The composition of claim 1 , wherein the first array of HLA protein spots comprises the HLA proteins at a concentration of 5 μg/ml-500 μg/ml.7. The composition of claim 1 , further comprising a second array of HLA protein spots indirectly attached to the surface of the substrate claim 1 , wherein the second array of HLA protein spots comprises different HLA proteins than the first array of HLA ...

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04-09-2014 дата публикации

Polypeptides and their use

Номер: US20140249052A1

The present invention provides polypeptides that bind to inorganic solid surfaces, structures comprising such polypeptides, and methods of making such structures.

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15-06-2017 дата публикации

AU MULTICOMPONENT NANOMATERIALS AND SYNTHESIS METHODS

Номер: US20170168045A1
Принадлежит:

A multicomponent nanomaterial AuNP(DTDTPA)(Ga), where DTDTPA is an amino-carboxylate ligand (diethylene triamine pentaacetic acid, DTPA) linked to the surface of the Au nanoparticle (NP) via dithiol (DT) linkage. Another embodiment is a multicomponent nanomaterial AuNP(DTDTPA)(Ga) with a biomolecule attached. In preferred embodiments, the Ga is Ga-67 or Ga-68. Preferred synthesis methods are conducted at room temperature. 1. A multicomponent nanomaterial , comprising at least one of the following nanoconstruct: AuNP(DTDTPA)(Ga) , AuNP(DTDTPA)(biomolecule) and AuNP(DTDTPA)(Ga)(biomolecule) , where DTDTPA is an amino-carboxylate ligand (diethylene triamine pentaacetic acid , DTPA) linked to the surface of the Au nanoparticle (NP) via dithiol (DT) linkage , and the biomolecule is selected from the group consisting of a peptide , antibody , ScFv antibody , the Fab portion of an antibody , affibody , enzyme , protein and a molecule comprising an amine group.2. The nanomaterial of claim 1 , comprising AuNP(DTDTPA)(Ga)(biomolecule).3. The nanomaterial of claim 2 , wherein the ratio of Au:Ga is in the range from 1:5 to 1:1.1254. The nanomaterial of claim 3 , wherein the ratio of Au:Ga is 1:5.5. The nanomaterial of in solution in a concentration in a range of 30 μg/ml to 5 mg/ml with a pH in a range of 6 to 13.6. The nanomaterial of in solution in a concentration in a range of 30 μg/ml to 5 mg/ml with a pH in a range of 6 to 13.7. The nanomaterial of claim 1 , comprising AuNP(DTDTPA)(Ga)(biomolecule) claim 1 , wherein the Ga comprises Ga-67.8. The nanomaterial of claim 1 , comprising AuNP(DTDTPA)(Ga)(biomolecule) claim 1 , wherein the Ga comprises Ga-68.9. A method for synthesis of a multicomponent nanomaterial claim 1 , the method comprising:{'sub': 3', '3, 'mixing an aqueous solution of one of the following: a biomolecule or Ga(NO)with AuNP(DTDTPA) conjugate dissolved in a buffer at room temperature and continually stirring the mixed solution for a predetermined time ...

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11-09-2014 дата публикации

Capture, purification, and release of biological substances using a surface coating

Номер: US20140255976A1
Принадлежит: Individual

This invention relates to a surface coating for capture circulating rare cells, comprising a nonfouling composition to prevent the binding of non-specific cells and adsorption of serum components; a bioactive composition for binding the biological substance, such as circulating tumor cells; with or without a linker composition that binds the nonfouling and bioactive compositions. The invention also provide a surface coating for capture and purification of a biological substance, comprising a releasable composition to release the non-specific cells and other serum components; a bioactive composition for binding the biological substance, such as circulating tumor cells; with or without a linker composition that binds the releasable and bioactive compositions. The present invention also discloses a novel microfluidic chip, with specific patterned microstructures to create a flow disturbance and increase the capture rate of the biological substance.

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11-09-2014 дата публикации

Method for immobilizing membrane proteins on surfaces

Номер: US20140256918A1
Принадлежит: SANOFI SA

Disclosed herein are methods for immobilizing membrane proteins or membrane protein complexes on analytical surfaces, which in some aspects comprise: obtaining a membrane protein or membrane protein complex comprising a capture moiety; immobilizing the membrane protein or membrane protein complex on the analytical surface by means of the capture moiety; and stabilizing at least one of the secondary, tertiary, or quaternary structures of the immobilized membrane protein or membrane protein complex by crosslinking with a crosslinking reagent. Also disclosed are analytical surfaces, which in some aspects comprise: a membrane protein or membrane protein complex comprising a capture moiety, wherein the membrane protein or membrane protein complex is immobilized on the analytical surface by means of the capture moiety, and wherein at least one of the secondary, tertiary, or quaternary structures of the membrane protein or membrane protein complex is stabilized by crosslinking.

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21-06-2018 дата публикации

INSULIN-LIPID COMPLEX, PREPARATION METHOD THEREFOR, AND PREPARATION THEREOF

Номер: US20180171031A1
Принадлежит:

Provided are an insulin-lipid complex, a preparation method thereof, and a formulation thereof. The insulin-lipid complex is prepared by compounding insulin and a lipid material in an organic solvent system containing a low boiling point acid, and drying. The mass ratio of insulin to the lipid material is 1:3-1:20. An oil solution of the insulin-lipid complex and vesicles containing insulin are further provided. 123.-. (canceled)24. A process for the preparation of an insulin-lipid complex , wherein the insulin-lipid complex is composed of insulin and lipid material and is not a liposome , the mass ratio of insulin to the lipid material being 1:3˜1:20 , and wherein the complex is prepared using an organic solvent system containing a low boiling point acid selected from the group consisting of trifluoroacetic acid and hydrogen chloride gas , or a combination thereof.25. The process for the preparation of an insulin-lipid complex according to claim 24 , wherein said insulin is selected from the group consisting of natural insulin claim 24 , porcine insulin claim 24 , bovine insulin claim 24 , recombinant human insulin and medium or long-acting insulin; and said lipid material is selected from the group consisting of natural phospholipids claim 24 , synthetic phospholipids claim 24 , cholesterol claim 24 , cholic acid and salts thereof.26. The process for the preparation of an insulin-lipid complex according to claim 25 , wherein said insulin is recombinant human insulin claim 25 , said lipid material is natural phospholipids claim 25 , and the mass ratio of insulin to the natural phospholipids is 1:5˜1:10.27. The process for the preparation of an insulin-lipid complex according to claim 24 , wherein said insulin-lipid complex further contains at least one selected from the groups consisting of antioxidants claim 24 , metal-chelators claim 24 , and protease inhibitors.28. The process for the preparation of an insulin-lipid complex according to claim 24 , wherein said ...

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28-06-2018 дата публикации

LIGAND IMMOBILIZATION METHOD

Номер: US20180179250A1
Принадлежит: KANEKA CORPORATION

A method for immobilizing a ligand on a formyl group-containing insoluble base material includes producing an imine by mixing the ligand and the formyl group-containing insoluble base material, and reducing the imine by using a borane complex, wherein the ligand comprises an amino group and has a specific affinity for a target compound, and wherein the borane complex has a Lewis base ligand having pKof 6.5 or less. 1. A method for immobilizing a ligand on a formyl group-containing insoluble base material , the method comprising:producing an imine by mixing the ligand and the formyl group-containing insoluble base material; andreducing the imine by using a borane complex,wherein the ligand comprises an amino group and has a specific affinity for a target compound, and{'sub': 'a', 'wherein the borane complex has a Lewis base ligand having pKof 6.5 or less.'}2. The method according to claim 1 , wherein the Lewis base ligand is one or more selected from the group consisting of a nitrogen-containing heterocyclic aromatic compound claim 1 , and an aromatic hydrocarbon compound having an amino group as a substituent.3. The method according to claim 1 , wherein the ligand is a peptide.4. The method according to claim 3 , wherein the ligand is an antibody affinity ligand.5. The method according to claim 4 , wherein the antibody affinity ligand is Protein A claim 4 , Protein G claim 4 , Protein L or an analog thereof.6. The method according to claim 1 , wherein the formyl group-containing insoluble base material is at least one selected from the group consisting of a polysaccharide claim 1 , a synthetic polymer and glass.7. The method according to claim 1 , wherein the formyl group-containing insoluble base material is cellulose or agarose.8. The method according to any one of claim 1 , wherein a form of the formyl group-containing insoluble base material is a porous bead claim 1 , a monolith or a porous membrane.9. A method for purifying a target compound claim 1 , ...

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18-09-2014 дата публикации

IMMUNOGENIC PEPTIDE CONJUGATE AND METHOD FOR INDUCING AN ANTI-INFLUENZA THERAPEUTIC ANTIBODY RESPONSE THEREWITH

Номер: US20140271650A1

Immunogenic influenza hemagglutinin-derived peptide conjugates described herein induce a specific therapeutic antibody response against influenza virus. The immunogenic peptide conjugates comprise a segment from the fusion initiation region (FIR) domain of an influenza hemagglutinin protein conjugated to an immunogenic carrier protein, such as keyhole limpet hemocyanin (KLH), bovine serum albumin (BSA), an influenza hemagglutinin (HA) protein (i.e., full length HA), and the like. The immunogenic peptide conjugates described herein can be utilized to treat or prevent influenza infection and to prepare influenza-specific therapeutic antibodies that interfere with influenza virus-host cell membrane fusion. The peptide conjugates can be formulated in pharmaceutical compositions useful for broad spectrum treatment or prevention of influenza infections. 1. An immunogenic peptide conjugate comprising a hemagglutinin fusion initiation region (FIR) peptide or a variant thereof , conjugated to an immunogenic carrier protein by a linking group; wherein the hemagglutinin FIR peptide has an amino acid sequence that consists of SEQ ID NO: 1 or a variant of SEQ ID NO: 1 sharing at least 50% sequence identity therewith and differing from SEQ ID NO: 1 by one or more amino acid substitutions selected from the group consisting of V1I , V1L , V1A , V1G , V1T , V1S , V1M , E2D , E2K , E2R , D3E , T4G , T4S , T4Q , T4A , K5F , K5M , K5I , K5V , K5L , K5A , I6L , I6V , I6A , I6T , I6S , I6Q , I6N , D7E , L8I , L8V , L8A , W9Y , S10T , S10G , S10A , S10M , and E14K.2. The peptide conjugate of wherein the immunogenic carrier protein is selected from the group consisting of the outer membrane protein complex of Neiserria meningitidis (OMPC) claim 1 , tetanus toxoid protein claim 1 , diphtheria toxin derivative CRM claim 1 , bovine serum albumin (BSA) claim 1 , cationized BSA claim 1 , Concholepas concholepas hemocyanin (CCH) claim 1 , hepatitis B virus (HBV) surface antigen protein (HBsAg) ...

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18-09-2014 дата публикации

NOVEL GLYCOCONJUGATES, GLYCOAMINO ACIDS, INTERMEDIATES THERETO, AND USES THEREOF

Номер: US20140271817A1

The present invention provides novel n-alkenyl glycosides and glycoconjugates, n-alkyl glycoamino acids, and methods for the synthesis thereof. In another aspect, the present invention provides novel clustered glycopeptides and methods for the synthesis thereof. In still another aspect, the present invention provides methods for the treatment of cancer, preferably for the prevention of recurrence of cancer, and methods for inducing antibodies in a subject, comprising administering to a subject in need, an effective amount of any of the inventive glycoconjugates as disclosed herein. 155-. (canceled)571. The glycopeptide of claim , which is conjugated to a carrier protein or lipid.59. The glycopeptide of claim 56 , wherein each occurrence of A is independently Globo-H claim 56 , fucosyl GM1 claim 56 , KH-1 claim 56 , glycophorin claim 56 , Le claim 56 , N3 claim 56 , Tn claim 56 , 2 claim 56 ,6-STn claim 56 , (2 claim 56 ,3)ST claim 56 , or TF claim 56 , with the proviso that at least one occurrence of A is Globo-H.60. The glycopeptide of claim 58 , wherein said glycopeptide has three occurrences of A comprising Tn claim 58 , Globo-H and Le.62. A pharmaceutical composition comprising:{'claim-ref': {'@idref': 'CLM-00058', 'claim 58'}, 'a glycopeptide of , and'}a pharmaceutically suitable carrier.63. A method of treating cancer in a subject suffering therefrom comprising:{'claim-ref': {'@idref': 'CLM-00062', 'claim 62'}, 'administering to a subject a therapeutically effective amount of a composition of .'}64. The method of claim 63 , wherein said method comprises preventing the recurrence of cancer in a subject.65. The method of claim 63 , wherein the cancer is a solid tumor.66. The method of claim 63 , further comprising co-administering one or more immunological adjuvants.67. The method of claim 66 , wherein at least one of said one or more immunological adjuvants is a saponin adjuvant.68. The method of claim 67 , wherein said saponin adjuvant is GPT-0100.69. The ...

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18-09-2014 дата публикации

METHODS AND COMPOSITIONS INVOLVING FIBRILLIZING POLYPEPTIDES FOR NANOFIBERS

Номер: US20140273148A1
Принадлежит:

Embodiments of the invention are directed to fibrillar adjuvants. For example, epitopes assembled by a synthetic peptide domain into nanofibers comprising a β-fibrillization peptide may elicit high antibody titers in the absence of any adjuvant. In certain embodiments, multiple different antigens may be integrated into polypeptide nanofibers, providing biomaterials with modular and precise composition of bioactive proteins. 1. A nanofiber complex composition , wherein the composition comprises a β-sheet nanofiber structure comprisinga) a plurality of non-β-sheet peptide tags, wherein a non-β-sheet peptide tag is attached to a compound; andb) a plurality of β-sheet peptides.2. The composition of claim 1 , wherein the structure comprises at least two different compounds.31. The composition of claim 1 , wherein the non-β-sheet peptides tags are α-helical peptides.4. The composition of claim 1 , wherein non-β-sheet peptides tags comprise one or more alpha helical motifs having a sequence of a b c d e f g claim 1 , with a and d being non-polar amino acids and e and g being charged amino acids.5. The composition of claim 4 , wherein a and/or d is Ala (A) claim 4 , Leu (L) claim 4 , Ile (I) claim 4 , Val (V) or a conservative derivative thereof in one or more of the alpha helical motifs.6. The composition of claim 4 , wherein a and/or d is Leu (L) in one or more of the alpha helical motifs.7. The composition of claim 4 , wherein e and/or g is Lys (K) claim 4 , Arg (R) claim 4 , His (H) claim 4 , Asp (D) claim 4 , Glu (E) or a conservative derivative thereof in one or more of the alpha helical motifs.89.-. (canceled)10. The composition of claim 4 , wherein one or more of b claim 4 , c claim 4 , and f is a hydrophobic amino acid in one or more of the alpha helical motifs.11. The composition of claim 4 , wherein one or more of b claim 4 , c claim 4 , and f in one or more of the alpha helical motifs is Val (V) claim 4 , Tyr (Y) claim 4 , Phe (F) claim 4 , Trp (W) claim 4 , Ile ...

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18-09-2014 дата публикации

IgG-BINDING PEPTIDE AND METHOD FOR DETECTING AND PURIFYING IgG USING SAME

Номер: US20140274790A1
Автор: Ito Yuji
Принадлежит:

Provided is a peptide that specifically or selectively binds to human IgG. This peptide comprises an amino acid sequence consisting of 13 to 17 amino acid residues and is capable of binding to human IgG, wherein the amino acid sequence is represented by formula I: (X)-C-(X)-H-R-G-(Xaa1)-L-V-W-C-(X), wherein, X each independently represents any amino acid residue except cysteine, C represents a cysteine residue, H represents a histidine residue, R represents an arginine residue, G represents a glycine residue, Xaa1 represents a glutamic acid residue or an asparagine residue, L represents a leucine residue, V represents a valine residue, and W represents a tryptophan residue. 117-. (canceled)18. A peptide comprising an amino acid sequence consisting of 13 to 17 amino acid residues , the peptide being capable of binding human IgG , wherein the amino acid sequence is represented by the following formula I:{'br': None, 'sub': 1-3', '1-3, '(X)-C-A-Y-H-R-G-E-L-V-W-C-(X)\u2003\u2003(I)'}wherein X each independently represents any amino acid residue except cysteine,C represents a cysteine residue,A represents an alanine residue,Y represents a tyrosine residue,H represents a histidine residue,R represents an arginine residue,G represents a glycine residue,E represents a glutamic acid residue,L represents a leucine residue,V represents a valine residue, andW represents a tryptophan residue.19. The peptide according to claim 18 , wherein claim 18 , when the peptide is 17 amino acid residues claim 18 , amino acid residues at positions 1 to 3 and 15 to 17 from an N terminus are each as follows:amino acid residue at position 1=S, O, F, or non-existent,amino acid residue at position 2=D, A, S, P, or non-existent,amino acid residue at position 3=S, D, T, N, E, or R,amino acid residue at position 15=S, T, or D,amino acid residue at position 16=H, G, Y, T, N, D, F, or non-existent, andamino acid residue at position 17=Y, F, H, M, or non-existent.21. The peptide according to claim 18 , ...

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05-07-2018 дата публикации

COUPLED PEPTIDE CHAIN FOR DISSOLVING POORLY SOLUBLE POLYPEPTIDES AND APPLICATION THEREOF FOR SEPARATION AND PURIFICATION IN LIQUID CHROMATOGRAPHY

Номер: US20180186830A1
Принадлежит:

The invention discloses a coupled peptide chain for dissolving poorly soluble polypeptides and an application thereof for separation and purification in liquid chromatography, belonging to the field of biochemistry. A special linker arm is used to link a hydrophilic polypeptide chain with a poorly soluble polypeptide chain to solve the problem that the poorly soluble polypeptide chains cannot be operated in the liquid chromatography, and optimize the combination of hydrophilic amino acids, and then the poorly soluble polypeptide chain and hydrophilic polypeptide chain are broken by hydrolyzing an ester bond, so that the target peptide chain is directly precipitated, the method has the characteristics of simplicity and high efficiency, and the poorly soluble polypeptide product obtained by the method fully meets the standards required by customers. 1. A coupled peptide chain for dissolving poorly soluble polypeptides , wherein the peptide chain is as shown in formula (I):{'br': None, 'sub': 'n', 'X-Ph-Y—(B)\u2003\u2003(I),'}wherein Ph represents a phenyl ring substituted at 1 and 4 positions;X represents a hydroxy group or a C1-C4 monohydroxy alkyl group;{'sub': 'n', 'Y represents a carbonyl group or a C2-C4 carbonylalkyl group formed after the dehydration and condensation reaction with (B);'}{'sub': 'n', '(B)represents a hydrophilic polypeptide chain formed by the condensation of n identical or different hydrophilic amino acids, and n is 1.2 to 2 times the number of amino acids of the poorly soluble polypeptide.'}2. A coupled peptide chain for dissolving poorly soluble polypeptides according to claim 1 , wherein{'sub': 2', '2', '2', '2', '2', '2', '2', '2', '2', '2, 'X is any one of a linear or branched —CHOH, —CHCHOH, —CHCHHOH or —CHCHCHCHOH; and'}{'sub': 2', '2', '2', '2', '2', '2, 'Y is any one of a linear or branched —CHCO—, —CHCHCO— or —CHCHCHCO—.'}3. A coupled peptide chain for dissolving poorly soluble polypeptides according to claim 2 , wherein the X-Ph-Y is ...

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13-07-2017 дата публикации

Capture, purification, and release of biological substances using a surface coating

Номер: US20170199184A1
Принадлежит: Academia Sinica

This invention relates to a surface coating for capture circulating rare cells, comprising a nonfouling composition to prevent the binding of non-specific cells and adsorption of serum components; a bioactive composition for binding the biological substance, such as circulating tumor cells; with or without a linker composition that binds the nonfouling and bioactive compositions. The invention also provide a surface coating for capture and purification of a biological substance, comprising a releasable composition to release the non-specific cells and other serum components; a bioactive composition for binding the biological substance, such as circulating tumor cells; with or without a linker composition that binds the releasable and bioactive compositions. The present invention also discloses a novel microfluidic chip, with specific patterned microstructures to create a flow disturbance and increase the capture rate of the biological substance.

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25-09-2014 дата публикации

COMPOSITIONS AND METHODS FOR RE-PROGRAMMING CELLS WITHOUT GENETIC MODIFICATION FOR REPAIRING CARTILAGE DAMAGE

Номер: US20140289882A1
Принадлежит:

The present inventions are directed to compositions and methods regarding the reprogramming of other cells (such as embryonic stem cells (ESCs), induced pluripotent stem cells (iPSCs), MSCs, fibroblasts, hematopoietic stem cells, endothelian stem cells, adipocytes, chondrocytes, osteoblasts, osteoclasts and endothelial cells) into chondrogenic cells without introducing exogenous genes to the samples. In particular, the present inventions are directed to transducible materials that are capable of transducing into the biological samples but are not genes or causing genetic modifications. The present inventions also are directed to methods of reprogramming the path of biological samples or treating diseases using the tranducible compositions thereof. 1. A transducible material comprising an effector domain , wherein the effector domain is a polypeptide , a small molecule , or a polynucleotide , and wherein the polypeptide is selected from the group consisting of Sox9 , Sox6 , Sox5 , c-Myc , Klf4 , Mef2C , Trps1 , Gli3 , Runx2 , Dlx5 , Dlx6 , GATA-6 , and Baf60c , and a homologous sequence thereof , and any combination thereof.2. The transducible material of claim 1 , further comprising a protein selected from the group consisting of Oct4 claim 1 , Klf4 claim 1 , Lin28 claim 1 , Nanog claim 1 , cMyc claim 1 , Ngn3 claim 1 , PDX1 claim 1 , MafA claim 1 , NeuroD claim 1 , Foxp3 claim 1 , Foxo1 claim 1 , Foxo3 claim 1 , a homologous sequence thereof claim 1 , and any combination thereof.3. The transducible material of claim 1 , wherein the homologous sequence means a sequence sharing at least 70% of identity in amino acid sequence with at least one member in the group.4. The transducible material of claim 3 , wherein the homologous sequence has substantially the same activity as at least one member in the group.5. The transducible material of further comprising a transduction domain.6. The transducible material of claim 5 , wherein the transduction domain is linked to the ...

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27-06-2019 дата публикации

DELIVERY OF AN AGENT TO AUTOPHAGIC AND APOPTOTIC CELLS BY VESICLES WITH A PROTEIN EXPRESSED ON SURFACE THEREOF

Номер: US20190194281A1
Принадлежит:

The invention creates engineered surface protein expression on vesicles for specific targeting and delivery of agents to autophagic and apoptotic cells. Moreover, the vesicles of the invention can achieve a synergistic effect on the targeting and drug delivery to autophagic and apoptotic cells and autophagic and apoptotic cells-containing tissues. 1. A protein-conjugated vesicle , comprising one or more lectins or a fragment thereof expressed or conjugated to the surface of the vesicle and optionally an agent.2. The vesicle of claim 1 , wherein the agent is encapsulated within the vesicle or attached to the outer surface of the vesicle.3. The vesicle of claim 1 , wherein the vesicle is a liposome or a micelle.4. The vesicle of claim 1 , wherein the vesicle is artificially engineered.5. The vesicle of claim 1 , wherein the one or more lectins or a fragment thereof is selected from the group consisting of: cation-dependent mannose-6-phosphate receptor (M6PR) claim 1 , P-selectin claim 1 , E-selectin claim 1 , L-selectin claim 1 , P-selectin-ligand-1 (PSGL-1) claim 1 , CD22 claim 1 , CD206 claim 1 , galectin 3 claim 1 , annexin V claim 1 , CD31 claim 1 , integrin αLβ2 claim 1 , VE-cadherin claim 1 , CD44 claim 1 , CD300a claim 1 , CD47 claim 1 , thrombospondin 1 (TSP1) and CD36 is used as a first protein.6. The vesicle of claim 1 , wherein the one or more lectins or a fragment thereof is selected from the group consisting of: CD300a claim 1 , CD47 claim 1 , thrombospondin 1 (TSP1) and CD36 claim 1 , Toll like receptor 4 (TLR4) or a fragment thereof is used as a second protein.7. The vesicle of claim 1 , which comprises one or more of the first protein of and one or more the second proteins of .8. The vesicle of claim 1 , which comprises M6PR in combination with P-selectin claim 1 , E-selectin claim 1 , PSGL-1 or galectin 3.9. The vesicle of claim 1 , which comprises Siglec 2 in combination with P-selectin claim 1 , galectin 3 or CD31.10. The vesicle of claim 1 , which ...

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27-06-2019 дата публикации

Synthetic Antibodies

Номер: US20190194358A1

The present invention provides methods for synthetic antibodies, methods for making synthetic antibodies, methods for identifying ligands, and related methods and reagents. 1. A multimeric peptide comprising a first affinity element conjugated to a second affinity element , wherein the first affinity element comprises a first peptide conjugated to a first DNA strand , the second affinity element comprises a second peptide conjugated to a second DNA strand , the first peptide and second peptide comprise a random combination of amino acids selected from the group of G , T , Q , K , S , W , L , and R; and the first affinity element is conjugated to the second affinity element by hybridization of the first DNA strand and the second DNA strand.2. The multimeric peptide of claim 1 , further comprising a first template DNA strand and a second template DNA strand wherein the at least one template DNA strand conjugates the first peptide with the first DNA strand and the at least one template DNA strand conjugates the second peptide with the second DNA strand.3. The multimeric peptide of claim 2 , wherein the first template DNA strand is conjugated to the first peptide at the C-terminus of the first peptide and the second template DNA strand is conjugated to the second peptide at the C-terminus of the second peptide.4. The multimeric peptide of claim 3 , wherein the first template DNA strand is conjugated to the first peptide using standard amine coupling chemistry and the second template DNA strand is conjugated to the second peptide using standard amine coupling chemistry.5. The multimeric peptide of claim 2 , wherein the first DNA strand is conjugated to the first peptide by conjugating with the first template strand and the second DNA strand is conjugated to the second peptide by conjugating with second template strand.6. The multimeric peptide of claim 5 , wherein the first DNA strand is conjugated to the first template strand by UV cross-linking and the second DNA ...

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02-10-2014 дата публикации

METHOD FOR SELECTING A CANDIDATE DRUG COMPOUND

Номер: US20140296478A1
Принадлежит: PEPSCAN SYSTEMS B.V.

The disclosure relates to the field of candidate drug testing and drug development. Described are methods for providing a compound composed of at least one molecule attached via at least two linkages to a molecular scaffold, the method comprising providing a scaffold comprising at least a first and a second reactive group; providing at least one molecule able to react with the at least first and second reactive group; and contacting the scaffold with at least one molecule to form at least two linkages between the scaffold and the molecule in a coupling reaction, wherein the formation of a linkage accelerates the formation of a consecutive linkage. The coupling reaction may be performed in solution, such as an aqueous solution. Furthermore, described is a method for selecting a candidate drug compound comprising providing a library of the compounds and determining the binding of a target molecule to the compounds. 1. A compound comprising at least two looped peptide structures attached via at least three thioether linkages to an aromatic or heteroaromatic molecule , wherein each of the at least three thioether linkages comprises a sulphur at a benzylic position on the aromatic or heteroaromatic molecule.2. The compound of claim 1 , wherein the aromatic or heteroaromatic molecule comprises a 5- or 6-membered aromatic or heteroaromatic ring.3. The compound of claim 1 , wherein each of the at least three thioether linkages is formed by reactinga halomethyl group on an aromatic or heteroaromatic ring withan SH functionality comprised within the peptide structure,thereby forming at least three thioether linkages, each comprising a sulphur at a benzylic position on said aromatic or heteroaromatic molecule.4. The compound of claim 3 , wherein the aromatic molecule is an arene.5. The compound of claim 1 , wherein each of the at least three thioether linkages is formed by reactingone of the halomethyl groups on a tris-, or tetrakis(halomethyl)-substituted aromatic or ...

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25-06-2020 дата публикации

COMPOSITIONS COMPRISING LIGANDS TO RHOB PROTEIN AND THE USES THEREOF

Номер: US20200200760A1
Принадлежит:

Methods and compositions are provided for diagnosing of autosomal-dominant polycystic kidney disease (ADPKD), chronic kidney diseases, kidney dysfunction, and preeclampsia in a subject, preferably in a urine sample of a human subject. The methods and compositions enable the detection or measurement in the sample or from a protein profile generated from the sample, of RhoB protein or peptide fragments thereof. Comparing the protein level(s) of the RhoB protein or peptide fragments thereof in the subject's sample with the level of the same protein or peptide(s) in a reference standard, permits the determination of a diagnosis of ADPKD and other said diseases, or the identification of a risk of developing ADPKD and other said diseases, or enables the monitoring of the status of progression or remission of ADPKD and other said diseases in the subject. 2. The method according to claim 1 , further comprising at least one step selected from:(d) after step (a), contacting the sample with a Second Ligand which is associated with a detectable label and which is capable of specifically complexing with, binding to, identifying or quantitatively detecting the First Ligand; and(e) performing a direct or indirect competitive ELISA, a direct or indirect competitive ELISPOT, a direct or indirect competitive MSD or a direct or indirect fluorescent immunoassay.3. (canceled)4. The method according to claim 1 , wherein the disease is autosomal-dominant polycystic kidney disease claim 1 , other chronic kidney diseases claim 1 , kidney dysfunction claim 1 , or preeclampsia.57-. (canceled)8. The method according to claim 1 , wherein said Ligand is covalently linked to a detectable label or immobilized on an immobilization substrate and which is capable of specifically complexing with claim 1 , binding to claim 1 , identifying or quantitatively detecting a Target within a RhoB protein.911-. (canceled)13. The method according to claim 1 , wherein the First Ligand is an antibody comprising ...

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23-10-2014 дата публикации

Antimicrobial peptides and uses thereof

Номер: US20140315789A1
Принадлежит: NEWSOUTH INNOVATIONS PTY LTD

The present disclosure relates generally to antimicrobial peptides, methods for their use, and methods for preparing devices having surfaces which are modified to incorporate OH said peptides. In some embodiments, the antimicrobial peptides are antimicrobial OH cationic peptides modified to comprise a thiol functional group.

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24-08-2017 дата публикации

METHOD FOR THE IMMOBILIZATION OF BIOMOLECULES

Номер: US20170241998A1
Принадлежит:

The invention relates to a method for the immobilization of biomolecules containing at least one sulfhydryl group, which method comprises contacting a modified metal surface with the biomolecule irradiating the resulting surface with UV radiation in the presence of a photo-initiator, wherein said metal surface is modified with a cross-linker compound comprising a terminal thiol or dithiol group covalently linked to the metal surface, a spacer group, which at the other terminal end is carrying an isolated double or triple bond. 1. A method for the immobilization of biomolecules containing at least one sulfhydryl group , which method comprises the steps of:a) optionally treating a biomolecule with an reducing agent in order to cleave existing —S—S— bridges in the biomolecule, orb) optionally treating a biomolecule with an acylation agent carrying a protected sulfhydryl group and de-protecting the sulfhydryl group;c) contacting a modified metal surface with the biomolecule; i) a terminal thiol or dithiol group covalently linked to the metal surface being connected to', 'ii) a spacer group, which at the other terminal end is carrying', 'iii) an isolated double or triple bond., 'd) irradiating the resulting surface with UV radiation in the presence of a photo-initiator, wherein said metal surface is modified with a cross-linker compound comprising2. A method according to claim 1 , wherein the linker compound is a compound of formula (I) claim 1 ,{'br': None, 'sub': 2', 'm', '2', 'p, 'HS—(CH)—CH(ZH)-SPACER-(CH)-A\u2003\u2003(I)'}in whichm is an integer from 2 to 6,{'sub': '2', 'A is selected from —CH═CHand —C≡CH, and'}Z is S or a single bond, [{'br': None, 'sub': 2', 'n', 'x', '2', '2', 'y', '2', 'r', 'v, '—(CH)—(C═O)—Y—(CHCH—O)—(CH)—(C═O)—X—'}, 'wherein', 'X and Y are each independently NH or O,', 'n is 0 or an integer from 1 to 10,', 'x and v are each independently 0 or 1,', 'y is an integer from 1 to 20,', 'r and p are each independently selected from an integer from 1 ...

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17-09-2015 дата публикации

ALLERGOIDS DERIVED FROM ALLERGENES

Номер: US20150259378A1
Принадлежит:

A method of making and a modified allergen having reduced allergenicity and preserved immunogenicity compared to corresponding native allergenic material. The preserved immunogenicity is elicited by a IgG-mediated antibody response, all or part of the primary amine groups of the lysine residues of the native allergenic material are functionalized with carbamoyl or thiocarbamoyl moieties, and all or part of the primary amine groups of the arginine residues of the carbamoyl- or thiocarbamoyl functionalized allergenic material are further functionalized with dialdehyde or diketal moieties. The raw allergenic material is selected from the group consisting of DP mites extract, Der p1, ovalbumin and Lipid Transfer Protein (LTP), the average percentage of modified primary amine groups of the lysine ranges between 75% and 100%; and the average percentage of the substituted arginine residues ranges between 25% and 10%. 112-. (canceled)14. The method according to claim 13 , further comprising the step of carring out said carbamylation reaction of step a) by reacting said native allergenic material with potassium cyanate to a final concentration of the salt ranging between 0.1 M and 1.5 M claim 13 , and by keeping a pH between 7 and 11 claim 13 , at a temperature ranging between the room temperature and 50° C. claim 13 , for a total reaction time ranging between 12 and 36 hours.15. The method according to claim 13 , further comprising the step of carrying out said carbamylation reaction of step a) by reacting said native allergenic material with potassium cyanate to a final concentration of the salt ranging between 0.4 M and 0.8 M claim 13 , and by keeping a pH between 9 and 9.6 claim 13 , at a temperature ranging between 35 and 40° C. claim 13 , for a total reaction time ranging between 16 and 24 hours.16. The method according to claim 13 , wherein claim 13 , between said step a) and said step b) claim 13 , the method further comprising the step of subjecting the thus- ...

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20-11-2014 дата публикации

Compositions and methods for entrapping protein on a surface

Номер: US20140342947A1
Автор: Michael E. Hogan
Принадлежит: Individual

The present invention provides a formulation to link protein to a solid support that comprises one or more proteins, Oligo-dT and one or more non-volatile, water-soluble protein solvents, solutes or combination thereof in an aqueous solution. Further provided is a method of attaching a protein to a surface of a substrate. The formulations provided herein are contacted onto the substrate surface, printed thereon and air dried. The substrate surface is irradiated with UV light to induce thymidine photochemical crosslinking via the thymidine moieties of the Oligo-dT.

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07-10-2021 дата публикации

POLYPEPTIDE DELIVERY COMPOSITION

Номер: US20210309763A1
Автор: WON Cheol Hee
Принадлежит:

A composition according to an embodiment of the present disclosure includes porous artificial chaperone particles having an average pore diameter of 1 to 100 nm, thereby stapling an alpha helical polypeptide to immobilize a random coiled tertiary-structure of the polypeptide into a stable alpha-helix structure, and significantly improving stability and efficiency of the polypeptide. 111-. (canceled)12: A composition comprising:porous artificial chaperone particles having an average pore diameter of 1 to 100 nm; andan alpha helical polypeptide supported and stapled inside of pores of the particle.13: The composition according to claim 12 , wherein the porous artificial chaperone particles have an average diameter of 150 to 1000 nm.14: The composition according to claim 12 , wherein a BET surface area of the porous artificial chaperone particles ranges from 200 to 700 m/g and a volume per g of pores ranges from 0.7 to 2.2 ml.15: The composition according to claim 12 , wherein the porous artificial chaperone particles are prepared by: reacting silica particles which have pores having a pore diameter of less than 5 nm with a swelling agent at 120 to 180° C. for 24 to 96 hours to expand the pores having a pore diameter of less than 5 nm; and calcining the silica particles having expanded pores at a temperature of 400° C. or higher for at least 3 hours.16: The composition according to claim 12 , wherein the porous artificial chaperone particles are characterized in that t claim 12 , at which an absorbance ratio in the following Equation 1 becomes ½ claim 12 , is 24 or more:{'br': None, 'sub': t', '0, 'A/A\u2003\u2003[Equation 1]'}{'sub': '0', 'wherein Ais absorbance of the porous artificial chaperone particles measured by putting 5 ml of suspension containing 1 mg/ml of porous artificial chaperone particles into a cylindrical permeable membrane having pores with a pore diameter of 50 kDa;'}15 ml of the same solvent as the suspension comes into contact with an outside of ...

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14-09-2017 дата публикации

IMMUNOGENIC PEPTIDE CONJUGATE AND METHOD FOR INDUCING AN ANTI-INFLUENZA THERAPEUTIC ANTIBODY RESPONSE THEREWITH

Номер: US20170258902A1
Принадлежит:

Immunogenic influenza hemagglutinin-derived peptide conjugates described herein induce a specific therapeutic antibody response against influenza virus. The immunogenic peptide conjugates comprise a segment from the fusion initiation region (FIR) domain of an influenza hemagglutinin protein conjugated to an immunogenic carrier protein, such asbovine serum albumin (BSA), an influenza hemagglutinin (HA) protein (i.e., full length HA), and the like. The immunogenic peptide conjugates described herein can be utilized to treat or prevent influenza infection and to prepare influenza-specific therapeutic antibodies that interfere with influenza virus-host cell membrane fusion. The peptide conjugates can be formulated in pharmaceutical compositions useful for broad spectrum treatment or prevention of influenza infections. 1Neiserria meningitidisConcholepas concholepas. An immunogenic peptide conjugate comprising a hemagglutinin fusion initiation region (FIR) peptide or a variant thereof , conjugated to an immunogenic carrier protein by a linking group; wherein the hemagglutinin FIR peptide has an amino acid sequence that consists of SEQ ID NO: 1 or a variant of SEQ ID NO: 1 sharing at least 50% sequence identity therewith and differing from SEQ ID NO: 1 by one or more amino acid substitutions selected from the group consisting of V1I , V1L , V1A , V1G , V1T , V1S , V1M , E2D , E2K , E2R , D3E , T4G , T4S , T4Q , T4A , K5F , K5M , K5I , K5V , K5L , K5A , I6L , I6V , I6A , I6T , I6S , I6Q , I6N , D7E , L8I , L8V , L8A , W9Y , S10T , S10G , S10A , S10M , and E14K; wherein the immunogenic carrier protein is selected from the group consisting of the outer membrane protein complex of (OMPC) , tetanus toxoid protein , diphtheria toxin derivative CRM , bovine serum albumin (BSA) , cationized BSA , hemocyanin (CCH) , hepatitis B virus (HBV) surface antigen protein (HBsAg) , HBV core antigen protein , a rotavirus capsid protein , bovine pappiloma virus (BPV) L1 protein , a human ...

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14-10-2021 дата публикации

APOLIPOPROTEIN NANODISCS WITH TELODENDRIMER

Номер: US20210317234A1
Принадлежит:

The present invention provides a nanodisc with a membrane scaffold protein. The nanodisc includes a membrane scaffold protein, a telodendrimer and a lipid. The membrane scaffold protein can be apolipoprotein. The telodendrimer has the general formula PEG-L-D-(R), wherein D is a dendritic polymer; L is a bond or a linker linked to the focal point group of the dendritic polymer; each PEG is a poly(ethylene glycol) polymer, each R is and end group of the dendritic polymer, or and end group with a covalently bound hydrophobic group, hydrophilic group, amphiphilic compound, or drug; and subscript n is an integer from 2 to 20. Cell free methods of making the nanodiscs are also provided. 1. A nanodisc comprising:a membrane scaffold protein;a telodendrimer;a lipid; anda hydrophobic drug.2. The nanodisc of claim 1 , wherein the membrane scaffold protein is apolipoprotein.3. The nanodisc of claim 1 , wherein the telodendrimer has the formula:{'br': None, 'sub': 'n', 'PEG-D-(R)'}whereinD is a dendritic polymer having a single focal group and a plurality of end groups;PEG is polyethyleneglycol (PEG) of 1-100 kDa linked to the focal group of the dendritic polymer;each R is independently selected from the group consisting of the end group of the dendritic polymer and an amphiphilic compound, such that when R is not an end group each R is linked to one of the end groups; andsubscript n is an integer from 2 to 20, wherein subscript n is equal to the number of end groups on the dendritic polymer, and wherein at least half the number n of R's are each an amphiphilic compound.4. The nanodisc of claim 3 , wherein the dendritic polymer is a poly(lysine) dendritic polymer wherein each end group is hydroxy.5. The nanodisc of claim 3 , wherein each amphiphilic compound is cholic acid (CA).6. The nanodisc of claim 5 , wherein the telodendrimer is selected from the group consisting of PEG-D-CA claim 5 , PEG-D-CAand PEG-D-CA claim 5 , wherein each dendritic polymer D is a poly(lysine) ...

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21-09-2017 дата публикации

Assay for High-Throughput Identification of Therapeutic Compounds

Номер: US20170268032A1
Принадлежит: Middle Tennessee State University

A solid supported branched linker assay system, including an alpha compound and a beta compounds reversibly tethered to a solid support; a branched linker coupled to the solid support that tethers the alpha and beta compounds to the solid support; the branched linker having two cleavable linkers that are chemically distinct from one another, wherein a first chemically distinct linker tethers the β compound to the branched linker and a second chemically distinct linker tethers the α compound to the branched linker; and at least two means for cleaving the chemically distinct linkers, wherein a first cleavage means is configured to selectively cleave a first chemically distinct linker and a second cleavage means is configured to selectively cleave a second chemically distinct linker.

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08-10-2015 дата публикации

SOLUBLE HYDROPHOBIC CORE CARRIER COMPOSITIONS FOR DELIVERY OF THERAPEUTIC AGENTS, METHODS OF MAKING AND USING THE SAME

Номер: US20150284476A1
Принадлежит: PharmaIN Corporation

The present invention relates to a soluble hydrophobic-core carrier composition comprising (i) a linear polymeric backbone; (ii) a plurality of hydrophilic polymeric protective chains covalently linked and pendant to the polymeric backbone and (iii) at least one hydrophobic moiety covalently linked and pendant to the polymeric backbone. In certain embodiments, the weight ratio of hydrophilic protective chains to hydrophobic moieties in the carrier is at least 15:1. In other embodiments, at least 90% of the residues of the polymeric backbone are coupled to a hydrophilic polymeric protective chain or a hydrophobic moiety. In other embodiments, the composition further comprises (iv) a hydrophobic load molecule dissociably linked to the hydrophobic moiety of the carrier. 1. A method of making a soluble hydrophobic-core carrier , comprising:step (a): contacting and reacting a carboxyl group or an alkyl carboxyl group of a hydrophilic polymeric protective chain with a carbodiimide reagent to provide a hydrophilic polymeric protective chain having an activated carboxyl group or an activated alkyl carboxyl group;{'sub': 2', '2, 'step (b): mixing and reacting a plurality of the hydrophilic polymeric protective chain having the activated carboxyl group or the activated alkyl carboxyl group of step (a) and a polymer comprising a linear polymeric backbone comprising NH-containing residues to provide a polymer comprising a linear polymeric backbone comprising a plurality of covalently-linked hydrophilic polymeric protective side chains and NH-containing residues;'}step (c): contacting and reacting a hydrophobic molecule comprising a free carboxyl group with a carbodiimide reagent to provide a hydrophobic molecule comprising an activated carboxyl group;{'sub': '2', 'step (d): mixing and reacting the hydrophobic molecule comprising the activated carboxyl group of step (c) and the polymer comprising the linear polymeric backbone comprising a plurality of covalently-linked ...

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29-09-2016 дата публикации

MASS SPECTROMETRIC ASSAYS FOR PEPTIDES

Номер: US20160282361A1
Автор: Anderson N. Leigh
Принадлежит: ANDERSON FORSCHUNG GROUP, INC.

Methods for interpretation of mass spectrometric tests for clinical biomarkers in which the amounts of internal standards are set to equal clinical evaluation thresholds, and preparations for adding stable isotope labeled peptide species to sample digests while minimizing losses and alterations in peptide stoichiometry. 1. A method of standardizing a quantitative mass spectrometric assay for a peptide analyte in a sample , comprising:adding a known amount of a SIS version of said analyte to a known amount of said sample, to form a standardized sample,measuring by mass spectrometry the relative amounts of said peptide analyte and said SIS version of said analyte in said standardized sample, andcomparing the amount of said peptide analyte to the amount of said SIS version of said analyte, wherein said known amount of said SIS version of said analyte corresponds to the analyte amount at a pre -determined test evaluation threshold.2. The method of claim 1 , wherein said test evaluation threshold is a clinical decision threshold derived from a clinical study establishing test sensitivity and specificity at said threshold.37-. (canceled)8. A method of standardizing a mass spectrometric assay for a protein or peptide analyte in a sample provided by a donor comprising:adding a known amount of a SIS version of said analyte as an internal standard to a known amount of said sample prior to mass spectrometric analysis;wherein said known amount of said internal standard corresponds to an analyte amount computed from one or more previous measurements of said analyte in one or more samples from said donor.9. A method of standardizing a mass spectrometric assay for a protein or peptide analyte in a sample comprising:adding known amounts of a first SIS version of said analyte and a second SIS version of said analyte as internal standards to a known amount of said sample prior to mass spectrometric analysis; wherein said known amount of said first SIS version corresponds to the ...

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25-12-2014 дата публикации

Immobilized Proteins and Methods and Uses Thereof

Номер: US20140378670A1
Принадлежит:

The invention relates to the field of covalently attaching proteins to a substrate, particularly to methods of immobilizing proteins by posttranslationally modifying a cysteine residue of said protein through the addition of functional groups. The invention also relates to biological molecules used in such techniques, including proteins, and detection methods and kits that utilize such immobilized proteins, such as a microdevice or “protein chip”, a high-throughput screening device, and for the microscopy of proteins on a surface. 1. A method of covalently immobilizing a protein , comprising:a. posttranslationally modifying a cysteine residue of said protein through the addition of functional groups, andb. immobilizing said protein by ligation of said functional groups to a substrate;wherein said protein comprises a soluble protein or a solubilized protein.2. The method of claim 1 , wherein said cysteine is in a C-terminal CaaX motif of a soluble protein.3. The method of claim 2 , where X is A claim 2 , S claim 2 , M claim 2 , L or Q.4. The method of claim 1 , wherein said posttranslational modification of a cysteine includes alkylation of the sulfhydryl moiety comprising one or more of catalysis of a farnesyl analog with protein farnesyltransferase and catalysis of a geranylgeranyl analog with protein geranylgeranyltransferase.5. The method of claim 4 , where said functional group comprises one or more of an azide claim 4 , an alkyne claim 4 , an alkene claim 4 , a ketone and an alkoxyamine.6. The method of claim 4 , wherein said farnesyl analog is selected from the analogs depicted in .7. The method of claim 1 , wherein said functional group comprises one or more of an azide and an alkyne.8. The method of claim 1 , wherein said substrate comprises one or more of a silicon surface selected from the group consisting of silicon claim 1 , glass claim 1 , SiO claim 1 , and silicon nitride claim 1 , a polymer surface comprising one or more of polymer beads and polymer ...

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03-09-2020 дата публикации

THERAPEUTIC CATIONIC PEPTIDES AND UNIMOLECULAR NANOPARTICLES FOR EFFICIENT DELIVERY THEREOF

Номер: US20200276130A1
Принадлежит: WISCONSIN ALUMNI RESEARCH FOUNDATION

Provided herein are peptides comprising an amino acid sequence having at least about 85% sequence identity to RYRPRAPIIAVT (SEQ ID NO: 1). These cationic peptides inhibit PKM2 methylation and may be used in the treatment of breast cancer and other diseases or conditions in which PKM2 is overexpressed. Such PKM2 peptides may be delivered to cancer cells using pH sensitive unimolecular nanoparticles comprising anionic polymers.

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22-10-2015 дата публикации

CONJUGATE FOR USE IN IMMUNOASSAY METHOD

Номер: US20150301038A1
Принадлежит: SEKISUI MEDICAL CO., LTD.

To adjust detection sensitivity and expand a measurement range depending on objects to be detected by a simple procedure in an immunoassay method involving using a colloidal metal having immobilized thereon an antibody or an antigen. Blocking treatment for a surface of a colloidal metal particle having immobilized thereon an antibody or an antigen with both components, i.e., a component of biological origin and a component of non-biological origin enables adjustment of measurement sensitivity with, for example, kinds and concentrations of both the components, and enables use of the component of non-biological origin, which has not been usable alone because of aggregation of a colloidal metal. 1. A conjugate , comprising a colloidal metal having a surface sensitized with an antibody or an antigen , wherein the surface of the colloidal metal is blocked with a component of non-biological origin and a component of biological origin.2Escherichia coli. The conjugate according to claim 1 , wherein the component of biological origin comprises one or more members selected from the group consisting of: BSA; casein; sericin; a polypeptide corresponding to amino acids 419 to 607 of an amino acid sequence of DnaK claim 1 , which is a heat shock protein (HSP) of origin; NEO PROTEIN SAVER; StartingBlock™ (PBS) Blocking Buffer; and Stabil Coat.3. The conjugate according to claim 1 , wherein the component of non-biological origin comprises one or more members selected from the group consisting of: a methacrylic acid polyoxyalkylene ester; NB4025; SN100; Stabil Guard; and Protein-Free Blocking Buffer.4. The conjugate according to claim 3 , wherein the methacrylic acid polyoxyalkylene ester comprises one or more members selected from the group consisting of: polyoxyethylene monomethacrylate; polyoxyethylene polyoxytetramethylene monomethacrylate; polyoxyethylene polyoxypropylene monomethacrylate; and octylpolyoxyethylene polyoxypropylene monomethacrylate.5. The conjugate according to ...

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19-10-2017 дата публикации

Methods of Lowering Serum Cholesterol

Номер: US20170296653A1
Принадлежит:

Methods of treating subjects having diseases, disorders, or conditions, including disorders associated with cholesterol homeostasis, responsive to agents modulating Kupffer cell function, including methods of administration and dosing regimens associated therewith, are provided. Methods of treating subjects having liver diseases, disorders, or conditions, including non-alcoholic steatohepatitis and non-alcoholic fatty liver disease, with an IL-10 agent are also provided. 1103.-. (canceled)104. A method of treating or preventing non-alcoholic steatohepatitis (NASH) or non-alcoholic fatty liver disease (NAFLD) in a subject , the method comprising:administering parenterally to a subject having NASH or NAFLD a therapeutically effective amount of a composition comprising PEGylated interleukin-10 (PEG-IL-10) agent.105. The method of claim 104 , wherein the PEG-IL-10 agent comprises mature human IL-10.106. The method of claim 104 , wherein the PEG-IL-10 agent comprises a variant of mature human IL-10 claim 104 , and wherein the variant exhibits activity comparable to the activity of mature human IL-10.107. The method of claim 104 , wherein said administering is effective to decrease cholesterol in the subject.108. The method of claim 104 , wherein said administering is effective to decrease triglycerides in the subject.109. The method of claim 104 , wherein said administering is effective to decrease peri-portal collagen deposition in the subject.110. The method of claim 104 , wherein said administering is effective to increase hepatocyte proliferation in the subject.111. The method of claim 104 , wherein said administering is subcutaneous.112. The method of claim 104 , wherein the method comprises administering at least one additional prophylactic or therapeutic agent.113. The method of claim 104 , wherein the PEG-IL-10 agent comprises at least one PEG molecule covalently attached to at least one amino acid residue of at least one subunit of IL-10.114. The method of claim ...

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19-10-2017 дата публикации

ANTI-TAU ANTIBODY AND USES THEREOF

Номер: US20170296680A1
Принадлежит: NATIONAL RESEARCH COUNCIL OF CANADA

The present invention relates to Tau-specific antibodies, fragments thereof, and uses thereof. More specifically, the present invention relates to Tau-specific antibodies, fragments thereof, and conjugates thereof with conjugated to a superparamagnetic nanoparticle. The molecules of the present invention may be used in visualizing damage from traumatic brain injury. 2. The isolated or purified antibody or fragment thereof of claim 1 , wherein the antibody comprisesa CDR1 sequence of GFTFSNFA (SEQ ID NO:1), a CDR2 sequence of IDNDGGRT (SEQ ID NO:2), and a a CDR3 sequence of AAMNLATRKWEL (SEQ ID NO:3); ora CDR1 sequence of GFTGDHYA (SEQ ID NO:4), a CDR2 sequence of IYSYSPNT (SEQ ID NO:5), and a CDR3 sequence of AADLEVAEYYAY (SEQ ID NO:6).4. The isolated or purified antibody or fragment thereof of any one of to claim 1 , wherein the antibody is a single-domain antibody (sdAb).5. The isolated or purified antibody or fragment thereof of claim 4 , wherein the sdAb is of camelid origin.6. The isolated or purified antibody or fragment thereof of any one of to claim 4 , wherein the antibody or fragment thereof is in a multivalent display format.7. The isolated or purified antibody or fragment thereof of claim 6 , wherein the antibody or fragment thereof is linked to a Fc claim 6 , Cdomain claim 6 , Cdomain claim 6 , Cdomain claim 6 , the hinge region claim 6 , or a combination thereof.8. A nucleic acid molecule encoding the isolated or purified antibody or fragment thereof of any one of to .9. A vector comprising the nucleic acid molecule of .10. The isolated or purified antibody or fragment thereof of any one of to claim 8 , wherein the antibody or fragment thereof is immobilized onto a surface.11. The isolated or purified antibody or fragment thereof of any one of to claim 8 , wherein the antibody or fragment thereof is linked to a cargo molecule.12. The isolated or purified antibody or fragment thereof of claim 11 , wherein the cargo molecule is a detectable agent claim ...

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12-11-2015 дата публикации

QUANTUM DOT-PROTEIN COMPLEXES, FILMS, AND METHODS OF USE

Номер: US20150323530A1
Автор: Wang Jinye
Принадлежит: EMPIRE TECHNOLOGY DEVELOPMENT LLC

The present application relates to protein-conjugated quantum dot compositions. The compositions may comprise, for example, zein proteins, and may be configured as films, for example on the sample-contacting surface of a sample well. Methods, kits, and an apparatus for the detection of food-borne microorganisms, for example, are also disclosed. 1. A composite material , comprising at least one quantum dot covalently bound to at least one prolamin protein , wherein the covalent bond is formed by the reaction of at least one carboxyl moiety or amino group on the surface of the quantum dot.2. The composite material of claim 1 , wherein the prolamin protein is a zein protein.3. (canceled)4. The composite material of claim 1 , wherein the quantum dot comprises a composition selected from the group comprising cadmium telluride claim 1 , cadmium selenium claim 1 , zinc sulfur claim 1 , lead selenium claim 1 , and rare earth doped colloidal phosphor nanoparticles.5. The composite material of claim 1 , wherein the quantum dot comprises cadmium telluride.6. The composite material claim 1 , further comprising at least one antibody.7. The composite material of claim 6 , wherein the antibody is bound to the protein.8. The composite material of claim 6 , wherein the antibody is configured to bind to a microorganism.9. A film comprising a plurality of quantum dots each covalently bound to at least one prolamin protein.10. The film of claim 9 , wherein the protein is a prolamin protein.11. The film of claim 9 , wherein the protein is a zein protein.12. The film of claim 9 , wherein the film is applied to a support structure.13. The film of claim 12 , wherein the support structure comprises a receptacle for holding a sample.14. The film of claim 9 , further comprising at least one antibody.15. The film of claim 14 , wherein the at least one antibody is bound to the protein.16. The film of claim 15 , wherein the antibody is configured to bind to a microorganism.1720-. (canceled)21. A ...

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02-11-2017 дата публикации

ENGINEERED POLYPEPTIDE CONJUGATES AND METHODS FOR MAKING THEREOF USING TRANSGLUTAMINASE

Номер: US20170313787A1
Принадлежит:

The present invention provides engineered polypeptide conjugates (e.g., antibody-drug-conjugates, toxin-(biocompatible polymer) conjugates, antibody-(biocompatible polymer) conjugates, and bispecific antibodies) comprising acyl donor glutamine-containing tags and amine donor agents. In one aspect, the invention provides an engineered Fc-containing polypeptide conjugate comprising the formula (Fc-containing polypeptide)-T-A, wherein T is an acyl donor glutamine-containing tag engineered at a specific site or comprises an endogenous glutamine made reactive by the Fc-containing polypeptide engineering, wherein A is an amine donor agent, and wherein the amine donor agent is site-specifically conjugated to the acyl donor glutamine-containing tag or the endogenous glutamine. The invention also provides methods of making engineered polypeptide conjugates using transglutaminase. 139-. (canceled)40. A method for preparing an engineered Fc-containing polypeptide conjugate comprising the formula: (Fc-containing polypeptide)-T-A , wherein T is an acyl donor glutamine-containing taq engineered at a specific site or comprises an endogenous glutamine (Q) made reactive by the Fc-containing polypeptide engineering; wherein A is an amine donor agent; wherein the amine donor agent is site-specifically conjugated to the acyl donor glutamine-containing taq or the endogenous glutamine at a carboxyl terminus , an amino terminus , or at an another site in the Fc-containing polypeptide , wherein the acyl donor glutamine-containing taq consists of an amino acid sequence selected from the group consisting of LLQGG (SEQ ID NO:2) , LSLSQG (SEQ ID NO:4) , GGGLLQGG (SEQ ID NO:5) , GLLQG (SEQ ID NO:6) , LLQ , GSPLAQSHGG (SEQ ID NO:7) , GLLQGGG (SEQ ID NO:8) , GLLQGG (SEQ ID NO:9) , GLLQ (SEQ ID NO:10) , LLQLLQGA (SEQ ID NO:47) , LLQGA (SEQ ID NO:48) , LLQYQGA (SEQ ID NO:49) , LLQGSG (SEQ ID NO:50) , LLQYQG (SEQ ID NO:51) , LLQLLQG (SEQ ID NO:52) , SLLQG (SEQ ID NO:53) , LLQLQ (SEQ ID NO:54) , ...

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