CA2694139C - Albumin binding polypeptide compositions - Google Patents
Albumin binding polypeptide compositions Download PDFInfo
- Publication number
- CA2694139C CA2694139C CA2694139A CA2694139A CA2694139C CA 2694139 C CA2694139 C CA 2694139C CA 2694139 A CA2694139 A CA 2694139A CA 2694139 A CA2694139 A CA 2694139A CA 2694139 C CA2694139 C CA 2694139C
- Authority
- CA
- Canada
- Prior art keywords
- albumin binding
- seq
- binding polypeptide
- polypeptide according
- albumin
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
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- C07K14/575—Hormones
- C07K14/61—Growth hormone [GH], i.e. somatotropin
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- C07K14/745—Blood coagulation or fibrinolysis factors
- C07K14/755—Factors VIII, e.g. factor VIII C (AHF), factor VIII Ag (VWF)
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- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C—CHEMISTRY; METALLURGY
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- Preparation Of Compounds By Using Micro-Organisms (AREA)
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- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
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| EP07113533.9 | 2007-07-31 | ||
| PCT/EP2008/059389 WO2009016043A2 (en) | 2007-07-31 | 2008-07-17 | New albumin binding compositions, methods and uses |
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Families Citing this family (83)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2012018687A1 (en) * | 2010-08-02 | 2012-02-09 | Macrogenics, Inc. | Covalent diabodies and uses thereof |
| CN104710518A (zh) * | 2007-07-31 | 2015-06-17 | 阿菲博迪公司 | 新白蛋白结合组合物、方法及应用 |
| US20120134984A1 (en) * | 2009-06-01 | 2012-05-31 | Olga Lubman | Molecules with extended half-lives and uses thereof |
| ES2641896T3 (es) * | 2010-03-08 | 2017-11-14 | Ge Healthcare Bioprocess R&D Ab | Polipéptido de unión a la región Fc de la inmunoglobulina G |
| KR20130093470A (ko) * | 2010-04-30 | 2013-08-22 | 가부시키가이샤산와카가쿠켄큐쇼 | 생리활성 물질 등의 생체 내 안정성 향상을 위한 펩티드 및 생체 내 안정성이 향상된 생리활성 물질 |
| DK2590993T3 (en) * | 2010-07-09 | 2015-06-29 | Affibody Ab | Polypeptides |
| BR122021020041B1 (pt) | 2010-09-28 | 2023-03-07 | Amylin Pharmaceuticals, Llc | Polipeptídeo quimérico, seu uso e composição que o compreende |
| JP6121330B2 (ja) * | 2010-09-28 | 2017-04-26 | アミリン・ファーマシューティカルズ, リミテッド・ライアビリティ・カンパニーAmylin Pharmaceuticals, Llc | 作用持続時間が増した改変ポリペプチド |
| CN103403024B (zh) | 2010-11-26 | 2017-08-11 | 分子组合公司 | 设计的锚蛋白重复蛋白的改进的n‑端加帽模块 |
| CN104080804B (zh) * | 2011-05-21 | 2017-06-09 | 宏观基因有限公司 | 去免疫化的血清结合结构域及其延长血清半衰期的用途 |
| JP6006309B2 (ja) * | 2011-07-08 | 2016-10-12 | アミリン・ファーマシューティカルズ, リミテッド・ライアビリティ・カンパニーAmylin Pharmaceuticals, Llc | 作用持続期間が増大し、免疫原性が減少した操作されたポリペプチド |
| WO2013009539A1 (en) | 2011-07-08 | 2013-01-17 | Amylin Pharmaceuticals, Inc. | Engineered polypeptides having enhanced duration of action and reduced immunogenicity |
| KR102336895B1 (ko) | 2012-02-20 | 2021-12-08 | 스위디쉬 오르펀 바이오비트럼 에이비 (피유비엘) | 인간 보체 c5에 결합하는 폴리펩티드 |
| WO2013148966A1 (en) * | 2012-03-28 | 2013-10-03 | Amylin Pharmaceuticals, Llc | Transmucosal delivery of engineered polypeptides |
| JP2020033372A (ja) * | 2012-03-28 | 2020-03-05 | アフィボディ・アーベー | 経口投与 |
| JP2015512902A (ja) * | 2012-03-28 | 2015-04-30 | アフィボディ・アーベー | 経口投与 |
| DK2855509T3 (en) | 2012-05-25 | 2018-07-23 | Janssen Biotech Inc | NON-NATURAL CONSENSUS ALBUMIN BINDING DOMAINS |
| JP6590695B2 (ja) * | 2012-09-25 | 2019-10-16 | アフィボディ・アーベー | アルブミン結合ポリペプチド |
| KR102191655B1 (ko) | 2012-10-05 | 2020-12-16 | 애피바디 에이비 | Her3 결합 폴리펩티드 |
| ES2674983T3 (es) | 2012-10-25 | 2018-07-05 | Affibody Ab | Método para la separación de proteínas que contienen un dominio que se une a albúmina |
| DK2912054T3 (en) * | 2012-10-25 | 2017-09-11 | Affibody Ab | Albumin-binding polypeptide |
| WO2014076179A1 (en) | 2012-11-14 | 2014-05-22 | Affibody Ab | New polypeptide |
| US9255262B2 (en) * | 2013-03-06 | 2016-02-09 | Vision Global Holdings Ltd. | Albumin-binding arginine deminase and the use thereof |
| USRE48805E1 (en) | 2013-03-06 | 2021-11-02 | Vision Global Holdings Ltd. | Method for cancer targeting treatment and detection of arginine using albumin-binding arginine deiminase fusion protein |
| EP2968490A1 (en) | 2013-03-14 | 2016-01-20 | Daiichi Sankyo Co., Ltd. | Novel binding proteins for pcsk9 |
| CA2902789A1 (en) | 2013-03-14 | 2014-09-18 | The Governing Council Of The University Of Toronto | Scaffolded peptidic libraries and methods of making and screening the same |
| ES2660912T3 (es) | 2013-03-15 | 2018-03-26 | Affibody Ab | Nuevos polipéptidos |
| US9943568B2 (en) | 2013-04-18 | 2018-04-17 | Armo Biosciences, Inc. | Methods of using pegylated interleukin-10 for treating cancer |
| US9823255B2 (en) | 2013-06-17 | 2017-11-21 | Armo Biosciences, Inc. | Method for assessing protein identity and stability |
| JP7138411B2 (ja) | 2013-08-28 | 2022-09-16 | アフィボディ・アーベー | 変異した骨格を有する結合ポリペプチド |
| HRP20210013T1 (hr) | 2013-08-28 | 2021-04-02 | Ipc Research, Llc | Stabilni polipeptidi koji se vezuju za ljudski komplement c5 |
| EP3038642A4 (en) | 2013-08-30 | 2017-01-18 | Armo Biosciences, Inc. | Methods of using interleukin-10 for treating diseases and disorders |
| EP3068425B1 (en) | 2013-11-11 | 2021-01-27 | Armo Biosciences, Inc. | Methods of using interleukin-10 for treating diseases and disorders |
| EP3083675B1 (en) | 2013-12-20 | 2018-03-07 | Affibody AB | Engineered albumin binding polypeptide |
| CN106573072A (zh) | 2014-06-02 | 2017-04-19 | 阿尔莫生物科技股份有限公司 | 降低血清胆固醇的方法 |
| MD20170020A2 (ro) | 2014-07-30 | 2017-07-31 | Ngm Biopharmaceuticals, Inc. | Compoziţii şi metode utilizate pentru tratamentul tulburărilor metabolice |
| KR102236830B1 (ko) | 2014-09-17 | 2021-04-06 | 애피바디 에이비 | 신규 폴리펩티드 |
| AU2015333827A1 (en) | 2014-10-14 | 2017-04-20 | Armo Biosciences, Inc. | Interleukin-15 compositions and uses thereof |
| CN107106655A (zh) | 2014-10-22 | 2017-08-29 | 阿尔莫生物科技股份有限公司 | 使用白细胞介素‑10治疗疾病和病症的方法 |
| US9920118B2 (en) | 2014-10-31 | 2018-03-20 | Ngm Biopharmaceuticals, Inc. | Compositions and methods of use for treating metabolic disorders |
| WO2016113246A1 (en) | 2015-01-12 | 2016-07-21 | Affibody Ab | Il-17a-binding polypeptides |
| US10618970B2 (en) | 2015-02-03 | 2020-04-14 | Armo Biosciences, Inc. | Method of treating cancer with IL-10 and antibodies that induce ADCC |
| WO2016179568A1 (en) * | 2015-05-06 | 2016-11-10 | Protomer Technologies, Inc. | Glucose responsive insulins |
| HK1248137A1 (zh) | 2015-05-28 | 2018-10-12 | 阿尔莫生物科技股份有限公司 | 用於治疗癌症的聚乙二醇化白细胞介素-10 |
| JP6882782B2 (ja) | 2015-08-04 | 2021-06-02 | デューク ユニバーシティ | 遺伝子コードされた本質的に無秩序な送達用ステルスポリマーおよびその使用方法 |
| WO2017035232A1 (en) | 2015-08-25 | 2017-03-02 | Armo Biosciences, Inc. | Methods of using interleukin-10 for treating diseases and disorders |
| US11752213B2 (en) | 2015-12-21 | 2023-09-12 | Duke University | Surfaces having reduced non-specific binding and antigenicity |
| CN107022031A (zh) * | 2016-01-29 | 2017-08-08 | 中国人民解放军军事医学科学院微生物流行病研究所 | 融合蛋白HSA1-Vβ1及其应用 |
| US11467156B2 (en) | 2016-06-01 | 2022-10-11 | Duke University | Nonfouling biosensors |
| JP2020500150A (ja) | 2016-09-23 | 2020-01-09 | デューク ユニバーシティ | 下限臨界溶液温度挙動を有する非反復かつ非構造的ポリペプチド |
| CN107952080A (zh) * | 2016-10-14 | 2018-04-24 | 中国科学院过程工程研究所 | 一种肿瘤靶向多肽-药物偶联衍生物、其制备方法及应用 |
| WO2018132732A1 (en) | 2017-01-12 | 2018-07-19 | Duke University | Genetically encoded lipid-polypeptide hybrid biomaterials that exhibit temperature triggered hierarchical self-assembly |
| WO2018213320A1 (en) | 2017-05-15 | 2018-11-22 | Duke University | Recombinant production of hybrid lipid-biopolymer materials that self-assemble and encapsulate agents |
| US11680083B2 (en) | 2017-06-30 | 2023-06-20 | Duke University | Order and disorder as a design principle for stimuli-responsive biopolymer networks |
| US11077199B2 (en) | 2017-08-09 | 2021-08-03 | Massachusetts Institute Of Technology | Albumin binding peptide conjugates and methods thereof |
| US20200239575A1 (en) * | 2017-10-06 | 2020-07-30 | University Of Utah Research Foundation | A fusion protein for targeted therapy of autoimmune disease |
| EP3691693A4 (en) | 2017-10-06 | 2021-08-25 | University Of Utah Research Foundation | FUSION PROTEIN FOR TARGETED THERAPY OF AUTOIMMUNE DISEASE |
| WO2019147954A1 (en) * | 2018-01-26 | 2019-08-01 | Duke University | Albumin binding peptide-drug (aibiped) conjugates and methods of making and using same |
| JP7545894B2 (ja) | 2018-03-13 | 2024-09-05 | アフィボディ アクティエボラーグ | 新規足場に基づくポリペプチド |
| EP3788343B1 (en) | 2018-04-30 | 2024-03-27 | Duke University | Stimuli-responsive peg-like polymer-based drug delivery platform |
| WO2020028806A1 (en) | 2018-08-02 | 2020-02-06 | Duke University | Dual agonist fusion proteins |
| WO2020051541A1 (en) * | 2018-09-07 | 2020-03-12 | Duke University | Nanoparticulate drug delivery systems |
| US12465640B2 (en) | 2019-02-25 | 2025-11-11 | The University Of Chicago | Methods and compositions for treating inflammatory and autoimmune conditions with ECM-affinity peptides linked to anti-inflammatory agents |
| WO2020245171A1 (en) | 2019-06-04 | 2020-12-10 | Molecular Partners Ag | Designed ankyrin repeat domain with improved stability |
| US11512314B2 (en) | 2019-07-12 | 2022-11-29 | Duke University | Amphiphilic polynucleotides |
| AU2020342349A1 (en) | 2019-09-02 | 2022-03-03 | Biotest Ag | Factor VIII protein with increased half-life |
| EP3785726A1 (en) | 2019-09-02 | 2021-03-03 | Biotest AG | Factor viii protein with increased half-life |
| US20220389066A1 (en) | 2019-11-05 | 2022-12-08 | Affibody Ab | Polypeptides |
| US20230190881A1 (en) | 2020-02-17 | 2023-06-22 | Biotest Ag | Subcutaneous administration of factor viii |
| EP3878515A1 (en) * | 2020-03-09 | 2021-09-15 | Hober Biotech AB | Therapeutic agent targeting her2 |
| WO2022098745A1 (en) | 2020-11-03 | 2022-05-12 | Indi Molecular, Inc. | Compositions, delivery systems, and methods useful in tumor therapy |
| WO2022098743A1 (en) | 2020-11-03 | 2022-05-12 | Indi Molecular, Inc. | Compositions, imaging, and therapeutic methods targeting folate receptor 1 (folr1) |
| US20240101605A1 (en) | 2020-12-21 | 2024-03-28 | Affibody Ab | New polypeptide |
| WO2022171892A1 (en) | 2021-02-15 | 2022-08-18 | Affibody Ab | New her2-binding polypeptide |
| AU2023218534A1 (en) | 2022-02-08 | 2024-07-11 | Affibody Ab | Protein z variants binding thymic stromal lymphopoietin and their medical use |
| AR129357A1 (es) | 2022-05-18 | 2024-08-14 | Protomer Tech Inc | Compuestos aromáticos que contienen boro y análogos de insulina relacionados |
| TW202416938A (zh) | 2022-08-10 | 2024-05-01 | 日商興和股份有限公司 | 親和體微胞(affibody micelle)藥物複合體 |
| TW202448926A (zh) | 2023-02-17 | 2024-12-16 | 比利時商艾伯霖克斯公司 | 結合新生兒fc受體之多肽 |
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| WO2025073871A1 (en) | 2023-10-03 | 2025-04-10 | Bicycletx Limited | Bicyclic peptide ligand complexes specific for tfr1 |
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| CN121041473A (zh) * | 2024-05-29 | 2025-12-02 | 烟台蓝纳成生物技术股份有限公司 | 一种双功能性融合蛋白、放射性核素标记物及其应用 |
| CN118666961B (zh) * | 2024-08-23 | 2024-11-26 | 通化安睿特生物制药股份有限公司 | 人白蛋白特异结合多肽及其应用 |
Family Cites Families (16)
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| SE509359C2 (sv) | 1989-08-01 | 1999-01-18 | Cemu Bioteknik Ab | Användning av stabiliserade protein- eller peptidkonjugat för framställning av ett läkemedel |
| FR2718452B1 (fr) * | 1994-04-06 | 1996-06-28 | Pf Medicament | Elément d'immunogène, agent immunogène, composition pharmaceutique et procédé de préparation. |
| FR2726471B1 (fr) * | 1994-11-07 | 1997-01-31 | Pf Medicament | Procede pour ameliorer l'immunogenicite d'un compose immunogene ou d'un haptene et application a la preparation de vaccins |
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| GB9911287D0 (en) * | 1999-05-14 | 1999-07-14 | Affibody Technology Sweden Ab | Self-assembling protein structures |
| EP2180054A1 (en) | 1999-12-24 | 2010-04-28 | Genentech, Inc. | Methods and compositions for prolonging elimination half-times of bioactive compounds |
| US20040001827A1 (en) | 2002-06-28 | 2004-01-01 | Dennis Mark S. | Serum albumin binding peptides for tumor targeting |
| CN1169827C (zh) | 2001-08-07 | 2004-10-06 | 沈阳三生制药股份有限公司 | 一种增强多肽在体内稳定性药物的生产方法及其应用 |
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- 2008-07-17 US US12/452,731 patent/US8937153B2/en active Active
- 2008-07-17 DE DE08786222T patent/DE08786222T1/de active Pending
-
2014
- 2014-11-24 US US14/551,931 patent/US10118949B2/en active Active
-
2015
- 2015-12-02 HK HK15111838.6A patent/HK1211040A1/xx unknown
Also Published As
| Publication number | Publication date |
|---|---|
| JP2010534486A (ja) | 2010-11-11 |
| US8937153B2 (en) | 2015-01-20 |
| EP2190863A2 (en) | 2010-06-02 |
| EP2190863B1 (en) | 2015-09-02 |
| ES2346178T1 (es) | 2010-10-13 |
| JP5718638B2 (ja) | 2015-05-13 |
| US10118949B2 (en) | 2018-11-06 |
| AU2008281913B2 (en) | 2013-11-07 |
| WO2009016043A2 (en) | 2009-02-05 |
| DK2190863T3 (en) | 2015-11-30 |
| WO2009016043A3 (en) | 2009-06-04 |
| US20100273979A1 (en) | 2010-10-28 |
| HK1211040A1 (en) | 2016-05-13 |
| EP2546261A3 (en) | 2013-08-14 |
| AU2008281913A1 (en) | 2009-02-05 |
| CN104710518A (zh) | 2015-06-17 |
| CN101765608B (zh) | 2015-03-11 |
| EP2546261A2 (en) | 2013-01-16 |
| CN101765608A (zh) | 2010-06-30 |
| ES2346178T3 (es) | 2015-11-02 |
| US20150158916A1 (en) | 2015-06-11 |
| CA2694139A1 (en) | 2009-02-05 |
| DE08786222T1 (de) | 2010-11-25 |
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