CA2897334A1 - Compositions and methods for increasing the serum half-life of a therapeutic agent targeting complement c5 - Google Patents
Compositions and methods for increasing the serum half-life of a therapeutic agent targeting complement c5 Download PDFInfo
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- CA2897334A1 CA2897334A1 CA2897334A CA2897334A CA2897334A1 CA 2897334 A1 CA2897334 A1 CA 2897334A1 CA 2897334 A CA2897334 A CA 2897334A CA 2897334 A CA2897334 A CA 2897334A CA 2897334 A1 CA2897334 A1 CA 2897334A1
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- C—CHEMISTRY; METALLURGY
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/113—Non-coding nucleic acids modulating the expression of genes, e.g. antisense oligonucleotides; Antisense DNA or RNA; Triplex- forming oligonucleotides; Catalytic nucleic acids, e.g. ribozymes; Nucleic acids used in co-suppression or gene silencing
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- A—HUMAN NECESSITIES
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- A61K2039/545—Medicinal preparations containing antigens or antibodies characterised by the dose, timing or administration schedule
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/94—Stability, e.g. half-life, pH, temperature or enzyme-resistance
Landscapes
- Health & Medical Sciences (AREA)
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- Chemical & Material Sciences (AREA)
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- Animal Behavior & Ethology (AREA)
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- Diabetes (AREA)
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- Biotechnology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Mycology (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Physical Education & Sports Medicine (AREA)
- Pulmonology (AREA)
- Neurology (AREA)
- Cardiology (AREA)
- Heart & Thoracic Surgery (AREA)
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Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201361806687P | 2013-03-29 | 2013-03-29 | |
| US61/806,687 | 2013-03-29 | ||
| PCT/US2014/032209 WO2014160958A1 (en) | 2013-03-29 | 2014-03-28 | Compositions and methods for increasing the serum half-life of a therapeutic agent targeting complement c5 |
Publications (1)
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| CA2897334A1 true CA2897334A1 (en) | 2014-10-02 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
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| CA2897334A Abandoned CA2897334A1 (en) | 2013-03-29 | 2014-03-28 | Compositions and methods for increasing the serum half-life of a therapeutic agent targeting complement c5 |
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| EP (2) | EP3473272A1 (OSRAM) |
| JP (2) | JP6505079B2 (OSRAM) |
| CA (1) | CA2897334A1 (OSRAM) |
| ES (1) | ES2768648T3 (OSRAM) |
| WO (1) | WO2014160958A1 (OSRAM) |
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| CA2647846C (en) | 2006-03-31 | 2016-06-21 | Chugai Seiyaku Kabushiki Kaisha | Methods for controlling blood pharmacokinetics of antibodies |
| CN106519025B (zh) | 2007-09-26 | 2021-04-23 | 中外制药株式会社 | 利用cdr的氨基酸取代来改变抗体等电点的方法 |
| CA2721052C (en) | 2008-04-11 | 2023-02-21 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to two or more antigen molecules repeatedly |
| BR112013013354A2 (pt) | 2010-11-30 | 2020-10-06 | Chugai Seiyaku Kabushiki Kaisha | molécula de ligação ao antígeno capaz de se ligar a uma pluralidade de moléculas de antígeno repetidamente |
| KR102605775B1 (ko) | 2013-03-14 | 2023-11-29 | 알닐람 파마슈티칼스 인코포레이티드 | 보체 성분 Ｃ5 ｉＲＮＡ 조성물 및 그 이용 방법 |
| EP3191591A1 (en) | 2014-09-12 | 2017-07-19 | Alnylam Pharmaceuticals, Inc. | Polynucleotide agents targeting complement component c5 and methods of use thereof |
| TWI617580B (zh) | 2014-12-19 | 2018-03-11 | 中外製藥股份有限公司 | 抗ｃ５抗體及使用方法 |
| MY181199A (en) | 2014-12-19 | 2020-12-21 | Chugai Pharmaceutical Co Ltd | Anti-myostatin antibodies, polypeptides containing variant fc regions, and methods of use |
| JP2018520139A (ja) * | 2015-06-26 | 2018-07-26 | アレクシオン ファーマシューティカルズ， インコーポレイテッド | エクリズマブまたはエクリズマブバリアントでのワクチン接種に従って患者を処置するための方法 |
| WO2017044811A1 (en) * | 2015-09-11 | 2017-03-16 | Bruce Andrien | Recombinant glycosylated eculizumab and eculizumab variants |
| MY196006A (en) | 2016-06-14 | 2023-03-06 | Regeneron Pharma | Anti-C5 Antibodies and Uses Thereof |
| WO2017217524A1 (en) * | 2016-06-17 | 2017-12-21 | Chugai Seiyaku Kabushiki Kaisha | Anti-c5 antibodies and methods of use |
| JP6527643B2 (ja) | 2016-08-05 | 2019-06-05 | 中外製薬株式会社 | Ｉｌ−８関連疾患の治療用又は予防用組成物 |
| ES2888904T3 (es) * | 2016-10-19 | 2022-01-10 | Alexion Pharma Inc | Un método de cuantificación de C5a sin unir en una muestra |
| WO2018075758A1 (en) * | 2016-10-19 | 2018-04-26 | Alexion Pharmaceuticals, Inc. | A method of quantitating unbound c5 in a sample |
| IL268327B2 (en) * | 2017-01-31 | 2025-09-01 | Chugai Pharmaceutical Co Ltd | Pharmaceutical preparation for use in the treatment and prevention of C5-related diseases and methods for the treatment and prevention of C5-related diseases |
| JP7209637B2 (ja) * | 2017-04-21 | 2023-01-20 | ヴォリューション イミュノ ファーマシューティカルズ エスエイ | 自己免疫性水疱症の治療のためのコバーシン |
| KR20200098528A (ko) | 2017-12-13 | 2020-08-20 | 리제너론 파아마슈티컬스, 인크. | 항-c5 항체 조합물 및 이의 용도 |
| EP3597222A1 (en) * | 2018-07-16 | 2020-01-22 | Easemedcontrol R & D GmbH & Co KG | Treatment and diagnosis of unresolved inflammatory diseases |
| EP3846850A4 (en) * | 2018-09-06 | 2022-06-15 | The Trustees of the University of Pennsylvania | HUMANIZED ANTI-C5 ANTIBODIES AND USES THEREOF |
| JP7654564B2 (ja) * | 2019-04-24 | 2025-04-01 | ザ トラスティーズ オブ ザ ユニバーシティ オブ ペンシルバニア | 二機能性ヒト化抗ｃ５抗体ならびにそのｈ因子融合タンパク質およびその使用 |
| WO2021154941A1 (en) * | 2020-01-31 | 2021-08-05 | Alnylam Pharmaceuticals, Inc. | Complement component c5 irna compositions for use in the treatment of amyotrophic lateral sclerosis (als) |
| US20240417725A1 (en) * | 2021-10-12 | 2024-12-19 | Vanqua Bio, Inc. | Oligonucleotides for targeting complement c5 |
Family Cites Families (43)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3710795A (en) | 1970-09-29 | 1973-01-16 | Alza Corp | Drug-delivery device with stretched, rate-controlling membrane |
| US4863457A (en) | 1986-11-24 | 1989-09-05 | Lee David A | Drug delivery device |
| US5116742A (en) | 1986-12-03 | 1992-05-26 | University Patents, Inc. | RNA ribozyme restriction endoribonucleases and methods |
| US4987071A (en) | 1986-12-03 | 1991-01-22 | University Patents, Inc. | RNA ribozyme polymerases, dephosphorylases, restriction endoribonucleases and methods |
| FR2650598B1 (fr) | 1989-08-03 | 1994-06-03 | Rhone Poulenc Sante | Derives de l'albumine a fonction therapeutique |
| US5164188A (en) | 1989-11-22 | 1992-11-17 | Visionex, Inc. | Biodegradable ocular implants |
| KR0185215B1 (ko) | 1990-11-30 | 1999-05-01 | 요시다 쇼오지 | 서방성 안구삽입용 약제 |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| FR2686901A1 (fr) | 1992-01-31 | 1993-08-06 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides antithrombotiques, leur preparation et compositions pharmaceutiques les contenant. |
| US5308341A (en) | 1993-09-28 | 1994-05-03 | Becton, Dickinson And Company | Method of testing the dose accuracy of a medication delivery device |
| US6074642A (en) | 1994-05-02 | 2000-06-13 | Alexion Pharmaceuticals, Inc. | Use of antibodies specific to human complement component C5 for the treatment of glomerulonephritis |
| US20030143204A1 (en) | 2001-07-27 | 2003-07-31 | Lewis David L. | Inhibition of RNA function by delivery of inhibitors to animal cells |
| JP4046354B2 (ja) | 1996-03-18 | 2008-02-13 | ボード オブ リージェンツ，ザ ユニバーシティ オブ テキサス システム | 増大した半減期を有する免疫グロブリン様ドメイン |
| US6146361A (en) | 1996-09-26 | 2000-11-14 | Becton Dickinson And Company | Medication delivery pen having a 31 gauge needle |
| WO1998023289A1 (en) | 1996-11-27 | 1998-06-04 | The General Hospital Corporation | MODULATION OF IgG BINDING TO FcRn |
| US6277375B1 (en) | 1997-03-03 | 2001-08-21 | Board Of Regents, The University Of Texas System | Immunoglobulin-like domains with increased half-lives |
| US6302855B1 (en) | 1998-05-20 | 2001-10-16 | Novo Nordisk A/S | Medical apparatus for use by a patient for medical self treatment of diabetes |
| US6192891B1 (en) | 1999-04-26 | 2001-02-27 | Becton Dickinson And Company | Integrated system including medication delivery pen, blood monitoring device, and lancer |
| US6277099B1 (en) | 1999-08-06 | 2001-08-21 | Becton, Dickinson And Company | Medication delivery pen |
| EP2275557A1 (en) | 2000-04-12 | 2011-01-19 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| PE20011227A1 (es) | 2000-04-17 | 2002-01-07 | Chiesi Farma Spa | Formulaciones farmaceuticas para inhaladores de polvo seco en la forma de aglomerados duros |
| CN100349629C (zh) | 2001-09-12 | 2007-11-21 | 贝克顿迪肯森公司 | 用于药物传送的微针为基础的笔装置和使用该装置的方法 |
| WO2003064621A2 (en) | 2002-02-01 | 2003-08-07 | Ambion, Inc. | HIGH POTENCY siRNAS FOR REDUCING THE EXPRESSION OF TARGET GENES |
| AU2003234336A1 (en) | 2002-05-03 | 2003-11-17 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and compositions for use in preparing sirnas |
| ITMI20021527A1 (it) | 2002-07-11 | 2004-01-12 | Consiglio Nazionale Ricerche | Anticorpi anti componente c5 del complemento e loro uso |
| JP4339852B2 (ja) | 2002-08-12 | 2009-10-07 | ニュー・イングランド・バイオラブズ・インコーポレイティッド | 遺伝子サイレンシングに関する方法および組成物 |
| US20050271660A1 (en) | 2002-09-06 | 2005-12-08 | Alexion Pharmaceuticals, Inc. | Nebulization of monoclonal antibodies for treating pulmonary diseases |
| US20040102469A1 (en) | 2002-09-13 | 2004-05-27 | Boehringer Ingelheim Pharma Gmbh & Co. Kg | Method for reducing the mortality rate |
| GB0222023D0 (en) | 2002-09-21 | 2002-10-30 | Aventis Pharma Ltd | Inhaler |
| US20050169921A1 (en) | 2004-02-03 | 2005-08-04 | Leonard Bell | Method of treating hemolytic disease |
| ES2674129T3 (es) | 2004-02-12 | 2018-06-27 | Archemix Llc | Agentes terapéuticos de base aptámeros útiles en el tratamiento de trastornos relacionados con complemento |
| US8685435B2 (en) | 2004-04-30 | 2014-04-01 | Allergan, Inc. | Extended release biodegradable ocular implants |
| US7919094B2 (en) | 2004-06-10 | 2011-04-05 | Omeros Corporation | Methods for treating conditions associated with MASP-2 dependent complement activation |
| DK1991275T3 (en) | 2006-03-08 | 2014-12-08 | Archemix Llc | Complement aptamers AND ANTI-C5 AGENTS FOR USE IN THE TREATMENT OF EYE DISEASES |
| HUE066795T2 (hu) | 2006-03-15 | 2024-09-28 | Alexion Pharma Inc | Paroxysmalis nocturnalis haemoglobinuriában szenvedõ betegek kezelése egy komplement inhibitorral |
| JP2010533181A (ja) | 2007-07-13 | 2010-10-21 | アボツト・バイオテクノロジー・リミテツド | ＴＮＦα阻害剤の肺投与のための方法及び組成物 |
| CA2721052C (en) | 2008-04-11 | 2023-02-21 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to two or more antigen molecules repeatedly |
| MX2011001371A (es) | 2008-08-05 | 2011-06-16 | Novartis Ag | Composiciones y metodos para anticuerpos que se dirigen a la proteina de complementos c5. |
| CA2742802C (en) | 2008-11-10 | 2019-11-26 | Alexion Pharmaceuticals, Inc. | Methods and compositions for treating complement-associated disorders |
| US20100291106A1 (en) | 2009-05-06 | 2010-11-18 | Novartis Ag | Compositions and methods for antibodies targeting complement protein c3b |
| US20110002931A1 (en) | 2009-06-23 | 2011-01-06 | Alexion Pharmaceuticals, Inc. | Bispecific antibodies that bind to complement proteins |
| BR112012022214A2 (pt) | 2010-03-01 | 2017-07-04 | Alexion Pharma Inc | métodos e composições para tratar doença de degos |
| KR102605775B1 (ko) | 2013-03-14 | 2023-11-29 | 알닐람 파마슈티칼스 인코포레이티드 | 보체 성분 Ｃ5 ｉＲＮＡ 조성물 및 그 이용 방법 |
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2014
- 2014-03-28 ES ES14722916T patent/ES2768648T3/es active Active
- 2014-03-28 WO PCT/US2014/032209 patent/WO2014160958A1/en not_active Ceased
- 2014-03-28 EP EP18211716.8A patent/EP3473272A1/en not_active Withdrawn
- 2014-03-28 CA CA2897334A patent/CA2897334A1/en not_active Abandoned
- 2014-03-28 JP JP2016505600A patent/JP6505079B2/ja active Active
- 2014-03-28 US US14/779,605 patent/US20160051673A1/en not_active Abandoned
- 2014-03-28 EP EP14722916.5A patent/EP2978451B1/en not_active Revoked
-
2018
- 2018-04-19 JP JP2018080510A patent/JP6505288B2/ja active Active
-
2019
- 2019-05-29 US US16/425,402 patent/US20200023060A1/en not_active Abandoned
-
2023
- 2023-10-06 US US18/482,159 patent/US20240293540A1/en active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| JP6505288B2 (ja) | 2019-04-24 |
| US20200023060A1 (en) | 2020-01-23 |
| EP3473272A1 (en) | 2019-04-24 |
| ES2768648T3 (es) | 2020-06-23 |
| JP6505079B2 (ja) | 2019-04-24 |
| US20240293540A1 (en) | 2024-09-05 |
| EP2978451B1 (en) | 2019-11-27 |
| EP2978451A1 (en) | 2016-02-03 |
| WO2014160958A1 (en) | 2014-10-02 |
| JP2016520542A (ja) | 2016-07-14 |
| US20160051673A1 (en) | 2016-02-25 |
| JP2018111728A (ja) | 2018-07-19 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Discontinued |
Effective date: 20180328 |