ES2567706T3 - Tetrapéptidos protectores para cuidado cutáneo - Google Patents
Tetrapéptidos protectores para cuidado cutáneo Download PDFInfo
- Publication number
- ES2567706T3 ES2567706T3 ES08844747.9T ES08844747T ES2567706T3 ES 2567706 T3 ES2567706 T3 ES 2567706T3 ES 08844747 T ES08844747 T ES 08844747T ES 2567706 T3 ES2567706 T3 ES 2567706T3
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- ES
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- Prior art keywords
- skin
- peptides
- plasmin
- peptide
- trypsin
- 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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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/10—Tetrapeptides
- C07K5/1024—Tetrapeptides with the first amino acid being heterocyclic
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
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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
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/08—Anti-ageing preparations
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
- A61K2800/74—Biological properties of particular ingredients
- A61K2800/78—Enzyme modulators, e.g. Enzyme agonists
- A61K2800/782—Enzyme inhibitors; Enzyme antagonists
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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
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
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- Dermatology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Birds (AREA)
- Epidemiology (AREA)
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- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Rheumatology (AREA)
- Pain & Pain Management (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US815 | 1979-01-04 | ||
| US81507P | 2007-10-29 | 2007-10-29 | |
| PCT/US2008/012191 WO2009058244A1 (en) | 2007-10-29 | 2008-10-28 | Protective skin care tetrapeptides |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2567706T3 true ES2567706T3 (es) | 2016-04-26 |
Family
ID=40305326
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES08844747.9T Active ES2567706T3 (es) | 2007-10-29 | 2008-10-28 | Tetrapéptidos protectores para cuidado cutáneo |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US8071555B2 (https=) |
| EP (1) | EP2205623B1 (https=) |
| JP (1) | JP5379806B2 (https=) |
| KR (1) | KR101668803B1 (https=) |
| CN (1) | CN101855235B (https=) |
| CA (1) | CA2701420C (https=) |
| ES (1) | ES2567706T3 (https=) |
| PL (1) | PL2205623T3 (https=) |
| WO (1) | WO2009058244A1 (https=) |
Families Citing this family (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8168181B2 (en) * | 2006-02-13 | 2012-05-01 | Alethia Biotherapeutics, Inc. | Methods of impairing osteoclast differentiation using antibodies that bind siglec-15 |
| CA2822302A1 (en) * | 2006-02-13 | 2007-08-23 | Alethia Biotherapeutics Inc. | Methods of impairing osteoclast differentiation |
| ES2421262T3 (es) * | 2007-11-30 | 2013-08-30 | Evonik Goldschmidt Gmbh | Composición para el cuidado personal y cosmética que contiene tetrapéptidos con las unidades CX1X2G, PX1X2P o PX1X2K |
| EP2723363B1 (en) | 2011-06-24 | 2018-08-29 | NoNO Inc. | Combination therapy for ischemia |
| US9241970B2 (en) * | 2011-12-13 | 2016-01-26 | Nono Inc. | Therapy for subarachnoid hemorrhage and ischemia |
| EP2838547B1 (en) * | 2012-04-16 | 2019-09-04 | Lubrizol Advanced Materials, Inc. | Compounds for the treatment and/or care of the skin and/or mucous membranes and their use in cosmetic or pharmaceutical compositions |
| HK1210192A1 (en) | 2012-07-19 | 2016-04-15 | Alethia Biotherapeutics Inc. | Anti-siglec-15 antibodies |
| CN105324122B (zh) * | 2013-06-14 | 2019-08-27 | 赫里克斯生物医疗公司 | 可用于治疗多种皮肤病的衍生自人类c-x-c趋化因子的四肽 |
| KR20150130616A (ko) * | 2014-05-13 | 2015-11-24 | (주)케어젠 | 피부상태 개선 활성을 갖는 펩타이드 및 이의 용도 |
| US9351911B1 (en) | 2015-07-30 | 2016-05-31 | Truth Aesthetics LLC | Topical skin care composition providing broad spectrum sunscreen |
| US9636292B2 (en) | 2015-07-30 | 2017-05-02 | Truth Aesthetics LLC | Topical skin care composition for night use |
| CN107629111B (zh) * | 2017-10-26 | 2021-06-04 | 陕西慧康生物科技有限责任公司 | 一种乙酰基四肽-2的液相合成方法 |
| CN113166205A (zh) * | 2018-11-30 | 2021-07-23 | 英特肽治疗有限公司 | 用于改善皮肤病状的多肽和方法 |
| KR102120992B1 (ko) * | 2019-05-03 | 2020-06-10 | (주)위바이오트리 | 신규한 금속 층상수산화물 복합체 및 이의 제조방법 |
| IT201900008364A1 (it) * | 2019-06-07 | 2020-12-07 | Espikem S R L | Peptidi bioattivi e composizioni che li comprendono |
| KR102778423B1 (ko) * | 2019-09-26 | 2025-03-10 | (주)아모레퍼시픽 | 피부 각질세포의 항노화 물질 스크리닝 방법, 스크리닝 키트 및 피부 각질세포의 항노화 물질 함유 조성물 |
| EP4001294A1 (en) * | 2020-11-17 | 2022-05-25 | The Boots Company plc | Tetrapeptide and compositions comprising tetrapeptides |
| FR3123193B1 (fr) * | 2021-05-28 | 2025-11-07 | Oreal | Procédé d’électroporation pour délivrer une composition comprenant au moins un peptide de poids moléculaire allant de 500 Da à 20 kDa |
| US20250268807A1 (en) * | 2022-04-27 | 2025-08-28 | Sbla Brands Inc. | Anti-aging peptide containing cosmetic |
| CN121717873A (zh) * | 2026-02-24 | 2026-03-24 | 中国医学科学院药用植物研究所 | 具有祛痘护肤作用的貂肽化合物及其分离制备 |
Family Cites Families (47)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB1357121A (en) * | 1970-07-28 | 1974-06-19 | Squibb & Sons Inc | Peptide enzyme inhibitors |
| GB2208511A (en) | 1987-08-07 | 1989-04-05 | Bayer Ag | Variants of bovine pancreatic trypsin inhibitor produced by recombinant dna technology |
| JP2820750B2 (ja) | 1988-04-21 | 1998-11-05 | ユーエービー リサーチ ファウンデイション | 創傷治療部位における癒着の発生からの保護に適するバイオエラストマー材料 |
| CA2032527C (en) | 1989-04-10 | 2002-07-02 | Jesse M. Jaynes | Lytic peptides: their use in the treatment of microbial infections, cancer and in the promotion of growth |
| US5561107A (en) | 1993-06-04 | 1996-10-01 | Demeter Biotechnologies, Ltd. | Method of enhancing wound healing by stimulating fibroblast and keratinocyte growth in vivo, utilizing amphipathic peptides |
| US5464820A (en) | 1993-06-22 | 1995-11-07 | The University Hospital | Specific inhibitors of tissue kallikrein |
| US5763576A (en) | 1995-10-06 | 1998-06-09 | Georgia Tech Research Corp. | Tetrapeptide α-ketoamides |
| FR2741076B1 (fr) | 1995-11-15 | 1998-01-30 | Rech De Pathologie Appliquee S | Conjugues peptidiques derives des hormones thymiques, leur utilisation a titre de medicament et compositions les contenant |
| EP0858808B1 (en) | 1997-01-17 | 2003-04-02 | Johnson & Johnson Medical Ltd. | Peptides for use in wound treatment |
| GB9702943D0 (en) | 1997-02-13 | 1997-04-02 | Univ Manchester | Wound healing |
| SE9701162D0 (sv) | 1997-03-27 | 1997-03-27 | Karolinska Innovations Ab | New use II |
| US6143742A (en) | 1997-12-11 | 2000-11-07 | Fuisz Technologies Ltd | Treatment for necrotizing infections |
| US6962904B1 (en) | 1998-03-13 | 2005-11-08 | Connective Tissue Imagineering | Elastin peptide analogs and uses thereof |
| US6344189B1 (en) | 1998-04-01 | 2002-02-05 | Biotech Australia Pty., Ltd. | Use of protease inhibitors for treating skin wounds |
| US6096327A (en) | 1998-11-05 | 2000-08-01 | Protease Sciences Inc. | Cosmetic compositions containing human type serine protease inhibitors for revitalizing the skin |
| CA2312075A1 (en) | 1998-11-05 | 2001-12-22 | Protease Sciences, Incorporated | Cosmetic compositions containing human type serine protease inhibitors |
| FR2788777B1 (fr) | 1999-01-22 | 2003-01-17 | Sederma Sa | Utilisation cosmetique ou dermopharmaceutique de peptides pour la regulation des dysfonctionnements immunologiques cutanes et dans l'inflammation cutanee induits par le vieillissement ou par les u.v. |
| US6492326B1 (en) | 1999-04-19 | 2002-12-10 | The Procter & Gamble Company | Skin care compositions containing combination of skin care actives |
| US6284802B1 (en) | 1999-04-19 | 2001-09-04 | The Procter & Gamble Company | Methods for regulating the condition of mammalian keratinous tissue |
| CA2276542C (en) | 1999-06-28 | 2013-07-30 | Vladislav I. Deigin | Novel peptide, a method for its preparation and a pharmaceutical composition containing the peptide |
| US6967023B1 (en) | 2000-01-10 | 2005-11-22 | Foamix, Ltd. | Pharmaceutical and cosmetic carrier or composition for topical application |
| US6537968B1 (en) | 2000-07-24 | 2003-03-25 | Alphamed Pharmaceuticals Corp | Treatment of lupus erythematosus |
| GB0029777D0 (en) | 2000-12-06 | 2001-01-17 | Regen Therapeutics Plc | Peptides |
| CA2441562C (en) | 2001-03-28 | 2013-05-14 | Helix Biomedix, Inc. | Short bioactive peptides and methods for their use |
| WO2002092623A1 (en) * | 2001-05-11 | 2002-11-21 | Research Development Foundation | INHIBITORS OF RECEPTOR ACTIVATOR OF NF-κB AND USES THEREOF |
| US20040167072A1 (en) | 2001-05-11 | 2004-08-26 | Aggarwal Bharat B. | Inhibitors of receptor activator of NF-kappaB and uses thereof |
| US7238656B2 (en) | 2001-08-29 | 2007-07-03 | Yissum Research Development Company Of The Hebrew University Of Jerusalem | Protective factors against inflammation, burns and noxious stimuli |
| US7041506B2 (en) | 2001-11-19 | 2006-05-09 | Becton Dickinson And Company | Peptides promoting cell adherence, growth and secretion |
| EP1534308A4 (en) | 2001-11-28 | 2007-03-14 | Becton Dickinson Co | PEPTIDES WITH INHIBITORY ACTION OF GROWTH |
| US20040009911A1 (en) | 2002-01-31 | 2004-01-15 | Irm, Llc | Hepsin substrates and prodrugs |
| US7491691B2 (en) | 2002-05-03 | 2009-02-17 | Sindrey Dennis R | Connective tissue stimulating peptides |
| US7265097B2 (en) | 2002-08-20 | 2007-09-04 | Chitogenics, Inc. | Methods of drug delivery using sulphated chitinous polymers |
| US7541440B2 (en) | 2002-09-30 | 2009-06-02 | Immunomedics, Inc. | Chimeric, human and humanized anti-granulocyte antibodies and methods of use |
| EP1686957B1 (en) | 2003-11-17 | 2012-03-07 | Sederma | Compositions containing mixtures of tetrapeptides and tripeptides |
| DE102004050563A1 (de) | 2004-10-15 | 2006-04-20 | Henkel Kgaa | Kosmetische und der dermatologische Zusammensetzungen mit Wirkstoffen für einen verbesserten Hautkomfort |
| DE102005000868A1 (de) | 2004-10-15 | 2006-04-20 | Henkel Kgaa | Zusammensetzungen mit Inhibitoren der Prostaglandin- und/oder Leukotrien-Synthese in Kombination mit Stimulatoren der Freisetzung kutaner Neuromediatoren |
| DE202004012807U1 (de) | 2004-08-13 | 2004-10-21 | Henkel Kgaa | Kosmetische und dermatologische Zusammensetzungen mit DNA-Reparaturenzymen und Oligopeptiden |
| DE102004055541A1 (de) | 2004-11-17 | 2006-05-18 | Henkel Kgaa | Kosmetische und dermatologische Zusammensetzungen zur Behandlung reifer Haut |
| US7271239B2 (en) | 2004-09-01 | 2007-09-18 | The Research Foundation Of State University Of New York | D-isomers of antimicrobial peptide |
| WO2006028993A2 (en) | 2004-09-02 | 2006-03-16 | Vanderbilt University | Assessment of cancer susceptibility to molecular targeted therapy by use of recombinant peptides |
| US20070224150A1 (en) | 2005-03-24 | 2007-09-27 | Yongji Chung | Growth factor for hair and skin treatment |
| FR2884418B1 (fr) | 2005-04-15 | 2008-11-21 | Soc Extraction Principes Actif | Utilisation d'un peptide comme principe actif amincissant |
| JP4846799B2 (ja) | 2005-07-05 | 2011-12-28 | バイオテンプト ベー.フェー. | 腫瘍の治療 |
| US20070077305A1 (en) | 2005-10-03 | 2007-04-05 | Le Tien C | Biocompatible polymeric matrix and preparation thereof |
| DE102005063062A1 (de) | 2005-12-29 | 2007-07-05 | Henkel Kgaa | Synergistische Proteinhydrolysat-Kombinationen zur Behandlung reifer Haut |
| US7807625B2 (en) | 2006-01-18 | 2010-10-05 | Grant Industries, Inc | Anti-wrinkle composition |
| EP2537932B1 (en) * | 2006-02-21 | 2016-04-27 | President and Fellows of Harvard College | Compositions for and methods of identifying antigens |
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2008
- 2008-10-28 CA CA2701420A patent/CA2701420C/en active Active
- 2008-10-28 PL PL08844747.9T patent/PL2205623T3/pl unknown
- 2008-10-28 KR KR1020107010739A patent/KR101668803B1/ko active Active
- 2008-10-28 JP JP2010531066A patent/JP5379806B2/ja active Active
- 2008-10-28 EP EP08844747.9A patent/EP2205623B1/en active Active
- 2008-10-28 CN CN2008801137748A patent/CN101855235B/zh active Active
- 2008-10-28 WO PCT/US2008/012191 patent/WO2009058244A1/en not_active Ceased
- 2008-10-28 US US12/290,236 patent/US8071555B2/en active Active
- 2008-10-28 ES ES08844747.9T patent/ES2567706T3/es active Active
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| CN101855235B (zh) | 2013-04-24 |
| CA2701420A1 (en) | 2009-05-07 |
| KR20100083828A (ko) | 2010-07-22 |
| EP2205623A1 (en) | 2010-07-14 |
| JP5379806B2 (ja) | 2013-12-25 |
| KR101668803B1 (ko) | 2016-10-24 |
| HK1146070A1 (zh) | 2011-05-13 |
| JP2011502121A (ja) | 2011-01-20 |
| PL2205623T3 (pl) | 2016-09-30 |
| US8071555B2 (en) | 2011-12-06 |
| WO2009058244A1 (en) | 2009-05-07 |
| CN101855235A (zh) | 2010-10-06 |
| EP2205623B1 (en) | 2016-03-16 |
| US20090142280A1 (en) | 2009-06-04 |
| CA2701420C (en) | 2016-02-09 |
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