JP5036533B2 - 持続放出製剤 - Google Patents
持続放出製剤 Download PDFInfo
- Publication number
- JP5036533B2 JP5036533B2 JP2007509735A JP2007509735A JP5036533B2 JP 5036533 B2 JP5036533 B2 JP 5036533B2 JP 2007509735 A JP2007509735 A JP 2007509735A JP 2007509735 A JP2007509735 A JP 2007509735A JP 5036533 B2 JP5036533 B2 JP 5036533B2
- Authority
- JP
- Japan
- Prior art keywords
- peptide
- complex
- pgg
- acid ester
- gallic acid
- 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.)
- Expired - Fee Related
Links
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Classifications
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- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
- A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/08—Peptides having 5 to 11 amino acids
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/54—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic compound
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/0012—Galenical forms characterised by the site of application
- A61K9/0019—Injectable compositions; Intramuscular, intravenous, arterial, subcutaneous administration; Compositions to be administered through the skin in an invasive manner
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Chemical & Material Sciences (AREA)
- Public Health (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Animal Behavior & Ethology (AREA)
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- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Gastroenterology & Hepatology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Organic Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US56524704P | 2004-04-23 | 2004-04-23 | |
| US60/565,247 | 2004-04-23 | ||
| PCT/US2005/014254 WO2005105057A1 (en) | 2004-04-23 | 2005-04-25 | Sustained release formulations |
Related Child Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2011196884A Division JP2012036194A (ja) | 2004-04-23 | 2011-09-09 | 持続放出製剤 |
| JP2011196883A Division JP5829870B2 (ja) | 2004-04-23 | 2011-09-09 | 持続放出製剤 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2007534698A JP2007534698A (ja) | 2007-11-29 |
| JP2007534698A5 JP2007534698A5 (enExample) | 2008-02-28 |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
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| US20050271726A1 (en) * | 2004-06-02 | 2005-12-08 | Albert Crum | Immune enhancing compositions and methods of use thereof |
| WO2006081171A1 (en) | 2005-01-24 | 2006-08-03 | Amgen Inc. | Humanized anti-amyloid antibody |
| US7252834B2 (en) * | 2005-04-25 | 2007-08-07 | Clemson University Research Foundation (Curf) | Elastin stabilization of connective tissue |
| MX2008001468A (es) * | 2005-06-30 | 2008-04-07 | Sod Conseils Rech Applic | Composiciones farmaceuticas del peptido similar al glucagon-1. |
| AU2007237163A1 (en) * | 2006-02-15 | 2007-10-18 | Gammacan Ltd. | Immunoglobulins from vitiligo plasma for melanoma therapy |
| EP2498096A1 (en) * | 2006-07-21 | 2012-09-12 | Amgen Inc. | Method of detecting and/or measuring hepcidin in a sample |
| US9610327B2 (en) | 2007-03-06 | 2017-04-04 | Amgen Inc. | Variant activin receptor polypeptides, alone or in combination with chemotherapy, and uses thereof |
| TW201718635A (zh) | 2007-03-06 | 2017-06-01 | 安美基公司 | 變異之活動素受體多肽及其用途 |
| MX2009012609A (es) | 2007-05-22 | 2009-12-07 | Amgen Inc | Composiciones y metodos para producir proteinas de fusion bioactivas. |
| WO2009085200A2 (en) | 2007-12-21 | 2009-07-09 | Amgen Inc. | Anti-amyloid antibodies and uses thereof |
| JP2011513220A (ja) * | 2008-02-21 | 2011-04-28 | ヴァトリックス・メディカル・インコーポレーテッド | デリバリービヒクルと組み合わせた結合組織安定剤の適用による動脈瘤の処置 |
| US20100016833A1 (en) * | 2008-07-15 | 2010-01-21 | Ogle Matthew F | Devices for the Treatment of Vascular Aneurysm |
| US20100119605A1 (en) * | 2008-11-12 | 2010-05-13 | Isenburg Jason C | Compositions for tissue stabilization |
| US8444624B2 (en) * | 2009-10-19 | 2013-05-21 | Vatrix Medical, Inc. | Vascular medical devices with sealing elements and procedures for the treatment of isolated vessel sections |
| US8911468B2 (en) | 2011-01-31 | 2014-12-16 | Vatrix Medical, Inc. | Devices, therapeutic compositions and corresponding percutaneous treatment methods for aortic dissection |
| PH12013501865A1 (en) | 2011-03-16 | 2014-01-06 | Amgen Inc | Potent and selective inhibitors of nav1.3 and nav1.7 |
| US9937255B2 (en) | 2011-05-18 | 2018-04-10 | Nectero Medical, Inc. | Coated balloons for blood vessel stabilization |
| EP3907237A1 (en) | 2012-12-20 | 2021-11-10 | Amgen Inc. | Apj receptor agonists and uses thereof |
| KR20150136061A (ko) | 2013-02-01 | 2015-12-04 | 산타 마리아 바이오테라퓨틱스, 인코포레이티드 | 대상에 항-액티빈-a 화합물의 투여 |
| WO2014165277A2 (en) | 2013-03-12 | 2014-10-09 | Amgen Inc. | POTENT AND SELECTIVE INHIBITORS OF Nav1.7 |
| US10941182B2 (en) | 2014-06-10 | 2021-03-09 | Amgen Inc. | Apelin polypeptides |
| WO2016020901A1 (en) | 2014-08-07 | 2016-02-11 | Acerta Pharma B.V. | Methods of treating cancers, immune and autoimmune diseases, and inflammatory diseases based on btk occupancy and btk resynthesis rate |
| US11318190B2 (en) | 2017-05-05 | 2022-05-03 | United States Government As Represented By The Department Of Veterans Affairs | Methods and compositions for treating liver disease |
| US11654114B2 (en) * | 2017-06-07 | 2023-05-23 | Egy-Nano Pharma, Lp | Oral prolonged drug delivery platforms |
| EP3829664A4 (en) | 2018-08-03 | 2022-05-04 | Nectero Medical, Inc. | PURIFIED PENTAGALLOYGLUCOSE AND DELIVERY DEVICES |
| WO2020227437A1 (en) | 2019-05-06 | 2020-11-12 | Axial Biotherapeutics, Inc. | Sustained release solid dosage forms for modulating the colonic microbiome |
| CN119326891B (zh) * | 2024-10-31 | 2025-07-01 | 中国人民解放军空军军医大学 | Ei24激动剂以及在制备抑制食管鳞癌增殖的制剂的应用 |
Family Cites Families (30)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US2849370A (en) * | 1953-06-04 | 1958-08-26 | Novo Terapeutisk Labortorium A | Injectable insulin preparations with protracted effect and process of producing same |
| GB929406A (en) | 1958-12-22 | 1963-06-19 | Upjohn Co | A process for the production of encapsulated material |
| CH498653A (fr) | 1968-03-29 | 1970-11-15 | Kobayashi Takehiko | Procédé d'encapsulation de matières hydrophobes |
| GB2209937B (en) * | 1987-09-21 | 1991-07-03 | Depiopharm S A | Water insoluble polypeptides |
| US5151265A (en) * | 1987-11-03 | 1992-09-29 | Genentech, Inc. | Gamma interferon formulation |
| US5019400A (en) | 1989-05-01 | 1991-05-28 | Enzytech, Inc. | Very low temperature casting of controlled release microspheres |
| WO1994008599A1 (en) | 1992-10-14 | 1994-04-28 | The Regents Of The University Of Colorado | Ion-pairing of drugs for improved efficacy and delivery |
| JP2744572B2 (ja) * | 1993-02-17 | 1998-04-28 | 鐘紡株式会社 | ポリフェノール化合物含有皮膚外用剤組成物の変色防止方法 |
| JPH06345668A (ja) * | 1993-06-07 | 1994-12-20 | Shibayagi:Kk | 感染防御組成物およびその用途 |
| US5922253A (en) | 1995-05-18 | 1999-07-13 | Alkermes Controlled Therapeutics, Inc. | Production scale method of forming microparticles |
| AU710347B2 (en) | 1995-08-31 | 1999-09-16 | Alkermes Controlled Therapeutics, Inc. | Composition for sustained release of an agent |
| WO1998010649A1 (en) | 1996-09-13 | 1998-03-19 | University Technology Corporation | Biocompatible cationic detergents and uses therefor |
| US20030190307A1 (en) * | 1996-12-24 | 2003-10-09 | Biogen, Inc. | Stable liquid interferon formulations |
| US6531154B1 (en) | 1997-06-10 | 2003-03-11 | Brown University Research Foundation | Modulated release from biocompatible polymers |
| JP2001510788A (ja) * | 1997-07-23 | 2001-08-07 | ペリオ プロダクツ リミテッド | 薬学的薬剤を薬学的に口腔内に制御放出するためのタンニン酸ポリマー組成物 |
| US6180666B1 (en) | 1997-09-05 | 2001-01-30 | Anmax, Inc. | Use of gallic acid esters to increase bioavailability of orally administered pharmaceutical compounds |
| US5962522A (en) | 1997-09-05 | 1999-10-05 | Avmax, Inc. | Propyl gallate to increase bioavailability of orally administered pharmaceutical compounds |
| US6613358B2 (en) | 1998-03-18 | 2003-09-02 | Theodore W. Randolph | Sustained-release composition including amorphous polymer |
| AU766959B2 (en) * | 1998-04-20 | 2003-10-30 | Genzyme Corporation | Drug delivery of proteins from polymeric blends |
| JP2000080027A (ja) * | 1998-09-02 | 2000-03-21 | Taiyo Kagaku Co Ltd | 徐放性製剤 |
| US6428818B1 (en) | 1999-03-30 | 2002-08-06 | Purdue Research Foundation | Tea catechin formulations and processes for making same |
| EP1225916A1 (en) | 1999-11-01 | 2002-07-31 | University Technology Corporation | Compositions and methods for controlled-release delivery and increased potency of pharmaceuticals via hydrophobic ion-pairing |
| US6713506B2 (en) * | 2000-10-11 | 2004-03-30 | University Of South Florida | Tea polyphenol esters and analogs thereof for cancer prevention and treatment |
| US6759064B2 (en) | 2001-02-22 | 2004-07-06 | Purdue Research Foundation | Compositions based on vanilloid-catechin synergies for prevention and treatment of cancer |
| JP5013152B2 (ja) * | 2001-02-28 | 2012-08-29 | 株式会社ビーエムジー | 蛋白質複合体形成剤 |
| US20040142048A1 (en) | 2002-02-22 | 2004-07-22 | Morre Dorothy M. | Compositions based on proanthocyanadin-catechin synergies for prevention and treatment of cancer |
| AU2003254544A1 (en) * | 2002-07-26 | 2004-02-23 | Dsm Ip Assets B.V. | Compositions comprising lactoferrin |
| US8912174B2 (en) * | 2003-04-16 | 2014-12-16 | Mylan Pharmaceuticals Inc. | Formulations and methods for treating rhinosinusitis |
| US7605120B2 (en) * | 2003-10-22 | 2009-10-20 | Amgen Inc. | Antagonists of the brandykinin B1 receptor |
| CN1997356A (zh) * | 2004-04-23 | 2007-07-11 | 安姆根有限公司 | 持续释放制剂 |
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- 2005-04-25 CN CN201410023256.4A patent/CN103920162B/zh not_active Expired - Fee Related
- 2005-04-25 PT PT57423154T patent/PT1750683E/pt unknown
- 2005-04-25 PL PL05742315T patent/PL1750683T3/pl unknown
- 2005-04-25 EP EP05742315A patent/EP1750683B1/en not_active Expired - Lifetime
- 2005-04-25 KR KR1020067021346A patent/KR101201638B1/ko not_active Expired - Fee Related
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- 2005-04-25 WO PCT/US2005/014254 patent/WO2005105057A1/en not_active Ceased
- 2005-04-25 SI SI200531678T patent/SI1750683T1/sl unknown
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| WO2005105057A1 (en) | 2005-11-10 |
| AU2005237542A1 (en) | 2005-11-10 |
| JP2007534698A (ja) | 2007-11-29 |
| US7323169B2 (en) | 2008-01-29 |
| CN103920162B (zh) | 2017-07-11 |
| ZA200609401B (en) | 2008-05-28 |
| SI1750683T1 (sl) | 2013-04-30 |
| KR20070026457A (ko) | 2007-03-08 |
| JP5829870B2 (ja) | 2015-12-09 |
| JP2012036194A (ja) | 2012-02-23 |
| CA2563185C (en) | 2010-04-20 |
| US20050271722A1 (en) | 2005-12-08 |
| US7732399B2 (en) | 2010-06-08 |
| KR101201638B1 (ko) | 2012-11-15 |
| EP1750683B1 (en) | 2013-01-09 |
| IL178596A0 (en) | 2007-02-11 |
| IL178596A (en) | 2012-06-28 |
| HK1103023A1 (en) | 2007-12-14 |
| AU2005237542B2 (en) | 2009-12-17 |
| DK1750683T3 (da) | 2013-04-15 |
| US20070292506A1 (en) | 2007-12-20 |
| CN103920162A (zh) | 2014-07-16 |
| EP1750683A1 (en) | 2007-02-14 |
| JP2012046520A (ja) | 2012-03-08 |
| HK1200092A1 (en) | 2015-07-31 |
| CN1997356A (zh) | 2007-07-11 |
| PL1750683T3 (pl) | 2013-05-31 |
| ES2400687T3 (es) | 2013-04-11 |
| CA2563185A1 (en) | 2005-11-10 |
| PT1750683E (pt) | 2013-01-25 |
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