ES2389285T3 - Péptidos bioactivos cortos y procedimientos para su uso - Google Patents

Péptidos bioactivos cortos y procedimientos para su uso Download PDF

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Publication number: ES2389285T3
Authority: ES; Spain
Prior art keywords: seq; peptides; peptide; flak; flak50
Prior art date: 2001-03-28
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 - Lifetime

Application number

ES09159563T

Other languages

English (en)

Spanish (es)

Inventor

Don R. Owen

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Helix Biomedix Inc

Original Assignee

Helix Biomedix Inc

Priority date (The priority date 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 date listed.)

2001-03-28

Filing date

2002-03-28

Publication date

2012-10-24

2001-03-28 Priority claimed from US09/820,053 external-priority patent/US6875744B2/en

2002-03-28 Application filed by Helix Biomedix Inc filed Critical Helix Biomedix Inc

2012-10-24 Application granted granted Critical

2012-10-24 Publication of ES2389285T3 publication Critical patent/ES2389285T3/es

2022-03-28 Anticipated expiration legal-status Critical

Status Expired - Lifetime legal-status Critical Current

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MYPYJXKWCTUITO-LYRMYLQWSA-N vancomycin Chemical compound O([C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=C2C=C3C=C1OC1=CC=C(C=C1Cl)[C@@H](O)[C@H](C(N[C@@H](CC(N)=O)C(=O)N[C@H]3C(=O)N[C@H]1C(=O)N[C@H](C(N[C@@H](C3=CC(O)=CC(O)=C3C=3C(O)=CC=C1C=3)C(O)=O)=O)[C@H](O)C1=CC=C(C(=C1)Cl)O2)=O)NC(=O)[C@@H](CC(C)C)NC)[C@H]1C[C@](C)(N)[C@H](O)[C@H](C)O1 MYPYJXKWCTUITO-LYRMYLQWSA-N 0.000 description 1
MYPYJXKWCTUITO-UHFFFAOYSA-N vancomycin Natural products O1C(C(=C2)Cl)=CC=C2C(O)C(C(NC(C2=CC(O)=CC(O)=C2C=2C(O)=CC=C3C=2)C(O)=O)=O)NC(=O)C3NC(=O)C2NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(CC(C)C)NC)C(O)C(C=C3Cl)=CC=C3OC3=CC2=CC1=C3OC1OC(CO)C(O)C(O)C1OC1CC(C)(N)C(O)C(C)O1 MYPYJXKWCTUITO-UHFFFAOYSA-N 0.000 description 1
108010026996 vishnu Proteins 0.000 description 1
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
239000003357 wound healing promoting agent Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/001—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof by chemical synthesis
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
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- A61P37/04—Immunostimulants
- A—HUMAN NECESSITIES
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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
- C07K14/43563—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4723—Cationic antimicrobial peptides, e.g. defensins
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
Medicinal Chemistry (AREA)
General Health & Medical Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Veterinary Medicine (AREA)
Public Health (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Pharmacology & Pharmacy (AREA)
Animal Behavior & Ethology (AREA)
Bioinformatics & Cheminformatics (AREA)
Engineering & Computer Science (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Molecular Biology (AREA)
Genetics & Genomics (AREA)
Biophysics (AREA)
Biochemistry (AREA)
Gastroenterology & Hepatology (AREA)
Zoology (AREA)
Oncology (AREA)
Tropical Medicine & Parasitology (AREA)
Communicable Diseases (AREA)
Toxicology (AREA)
Immunology (AREA)
Pulmonology (AREA)
Insects & Arthropods (AREA)
Dermatology (AREA)
Cardiology (AREA)
Hematology (AREA)
Heart & Thoracic Surgery (AREA)
Ophthalmology & Optometry (AREA)
Virology (AREA)
Endocrinology (AREA)
Reproductive Health (AREA)
Urology & Nephrology (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Peptides Or Proteins (AREA)

ES09159563T 2001-03-28 2002-03-28 Péptidos bioactivos cortos y procedimientos para su uso Expired - Lifetime ES2389285T3 (es)

Applications Claiming Priority (4)

Application Number	Priority Date	Filing Date	Title
US27950501P	2001-03-28	2001-03-28
US820053		2001-03-28
US09/820,053 US6875744B2 (en)	2001-03-28	2001-03-28	Short bioactive peptides
US279505		2001-03-28

Publications (1)

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ES2389285T3 true ES2389285T3 (es)	2012-10-24

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ES09159563T Expired - Lifetime ES2389285T3 (es)	2001-03-28	2002-03-28	Péptidos bioactivos cortos y procedimientos para su uso

Country Status (8)

Country	Link
US (1)	US7381704B2 (2)
EP (2)	EP1379265A4 (2)
JP (2)	JP4310107B2 (2)
KR (1)	KR100891157B1 (2)
AU (1)	AU2002255952A1 (2)
CA (1)	CA2441562C (2)
ES (1)	ES2389285T3 (2)
WO (1)	WO2002079408A2 (2)

Families Citing this family (30)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
AU2004229465B2 (en) *	2003-04-09	2010-04-29	The United States Of America Department Of Veterans Affairs	Compositions and methods related to production of erythropoietin
JP2005281225A (ja) *	2004-03-30	2005-10-13	Japan Science & Technology Agency	新規塩基性抗菌ペプチド及びその利用
JP2009502967A (ja) *	2005-07-27	2009-01-29	ナステックファーマスーティカルカンパニーインク．	粘膜送達を向上させるためのタイトジャンクション調節ペプチド化合物
US7601361B2 (en) *	2005-10-03	2009-10-13	E. I. Du Pont De Nemours And Company	Process for providing antimicrobial surfaces
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
US8586541B2 (en) *	2006-06-01	2013-11-19	Therapeutic Peptides, Inc.	Polymeric biosurfactants
ES2557402T3 (es)	2006-06-13	2016-01-25	Helix Biomedix Inc.	Fragmentos peptídicos para inducir la síntesis de proteínas de la matriz extracelular
KR100742982B1 (ko) *	2006-06-22	2007-07-26	케이맥(주)	초점 타원계측기
EP2125878B1 (en)	2007-01-05	2013-02-20	Helix Biomedix, Inc.	Short bio-active peptides for cellular and immunological modulation
CA2685720C (en) *	2007-05-01	2016-07-05	Fundacao De Amparo A Pesquisa Do Estado De Sao Paulo - Fapesp	Analgesic compounds
CA2701420C (en)	2007-10-29	2016-02-09	Helix Biomedix Inc.	Protective skin care tetrapeptides
GB0803352D0 (en)	2008-02-22	2008-04-02	Ntnu Technology Transfer As	Oligopeptidic compounds and uses thereof
EP2168591A1 (en) *	2008-09-24	2010-03-31	Helmholtz Zentrum München Deutsches Forschungszentrum für Gesundheit und Umwelt (GmbH)	Antimicrobial peptides
US20120270770A1 (en) *	2010-08-03	2012-10-25	Jesse Michael Jaynes	Anti-angiogenic peptides and their uses
HK1210192A1 (en)	2012-07-19	2016-04-15	Alethia Biotherapeutics Inc.	Anti-siglec-15 antibodies
ITBS20120126A1 (it) *	2012-08-01	2014-02-02	Paoli Ambrosi Gianfranco De	Composizione antibatterica per uso topico
WO2014040605A1 (en) *	2013-04-09	2014-03-20	Elawdan Khaled Mohey Eldin	New peptides as a monotherapy in malignancy control
GB201319620D0 (en)	2013-11-06	2013-12-18	Norwegian University Of Science And Technology	Immunosuppressive agents and their use in therapy
US10016480B2 (en)	2014-10-14	2018-07-10	The United States Of America, As Represented By The Secretary, Dept. Of Health And Human Services	Peptide-based methods for treating pancreatic cancer
CN105061562B (zh) *	2015-09-16	2018-01-12	山东电力中心医院	一种具有抗肺癌作用的寡肽及其应用
US9439917B1 (en)	2015-12-28	2016-09-13	Shetal Amit Shah	Anti-blepharitis compositions and their use
CA3014442A1 (en)	2016-02-29	2017-09-08	Dana-Farber Cancer Institute, Inc.	Stapled intracellular-targeting antimicrobial peptides to treat infection
AU2018304230A1 (en) *	2017-07-19	2020-02-06	Dana-Farber Cancer Institute, Inc.	Stabilized anti-microbial peptides for the treatment of antibiotic-resistant bacterial infections
BR112020017397A2 (pt) *	2018-04-30	2021-01-19	L'oreal	Peptídeo, composição para inibir a contração de células musculares, método para inibir a contração de células musculares, método para induzir a proliferação de células epidérmicas e método para reduzir a aparência de rugas
KR20210151945A (ko)	2019-04-12	2021-12-14	립타이드 바이오사이언스, 인코포레이티드	대식세포 활성을 조정하기 위한 방법
FR3099060B1 (fr) *	2019-07-26	2022-01-14	Bionuclei	Complexe hybride mineral et organique et son utilisation pour le maintien de l’equilibre microbiologique de la peau et/ou d’une composition cosmetique et/ou dermopharmaceutique
TR2023016596A2 (tr) *	2023-12-06	2024-01-22	Karadeniz Teknik Ueniversitesi Teknoloji Transferi Uygulama Ve Arastirma Merkezi Mueduerluegue	Anti̇bi̇yoti̇klere alternati̇f yeni̇ ki̇tosan konjuge anti̇mi̇krobi̇yal pepti̇ti̇n geli̇şti̇ri̇lmesi̇
WO2025157595A2 (en) *	2024-01-25	2025-07-31	Lipotrue, S.L.	Peptides and cosmetic compositions for use in the treatment of acne and its related skin conditions
CN120209088B (zh) *	2025-03-07	2026-03-03	黄小柯	一种多效蛋白mel3及其应用

Family Cites Families (18)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4355104A (en) *	1980-06-17	1982-10-19	Kabigen Ab	Bacteriolytic proteins
US4520016A (en) *	1980-06-17	1985-05-28	Kabigen Ab	Bacteriolytic proteins
US5861478A (en)	1987-07-06	1999-01-19	Helix Biomedix, Inc.	Lytic peptides
CA1327311C (en) *	1987-07-06	1994-03-01	Jesse M. Jaynes	Therapeutic antimicrobial polypeptides, their use and methods for preparation
WO1989000194A1 (en) *	1987-07-06	1989-01-12	Louisiana State University Agricultural And Mechan	Inhibition of eucaryotic pathogens and neoplasms and stimulation of fibroblasts and lymphocytes with lytic peptides
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
CA2107674A1 (en) *	1991-04-08	1992-10-09	W. Lee Maloy	Novel peptide compositions and uses therefor
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
WO1994028921A1 (en) *	1993-06-04	1994-12-22	Demeter Biotechnologies, Ltd.	Method of treating pulmonary disease states with non-naturally occurring amphipathic peptides
US5955573A (en)	1993-06-04	1999-09-21	Demegen, Inc.	Ubiquitin-lytic peptide fusion gene constructs, protein products deriving therefrom, and methods of making and using same
WO1995013085A1 (en)	1993-11-08	1995-05-18	Demeter Biotechnologies Ltd.	Methylated lysine-rich lytic peptides and method of making same by reductive alkylation
US5789542A (en) *	1994-04-22	1998-08-04	Board Of Supervisors Of Louisiana State University And Agricultural And Mechanical College	Amphipathic peptides
IL114697A0 (en)	1994-07-22	1995-11-27	Demeter Biotech Ltd	Polypeptides comprising ubiquitin-lytic peptide fusion protein products deriving therefrom their preparation and use
WO1997021728A1 (en) *	1995-12-12	1997-06-19	Karolinska Innovations Ab	PEPTIDE BINDING THE KLVFF-SEQUENCE OF AMYLOID $g(b)
US6566334B1 (en) *	1997-02-06	2003-05-20	Board Of Supervisors Of Louisiana State University And Agricultural And Mechanical College	Short amphipathic peptides with activity against bacteria and intracellular pathogens
US6635740B1 (en) *	1997-03-27	2003-10-21	Board Of Supervisors Of Louisiana State University And Agricultural And Mechanical College	Ligand/lytic peptide compositions and methods of use
US6958212B1 (en) *	1999-02-01	2005-10-25	Eidgenossische Technische Hochschule Zurich	Conjugate addition reactions for the controlled delivery of pharmaceutically active compounds
MXPA02006752A (es)	2000-01-06	2004-09-10	Monsanto Technology Llc	Preparacion de proteinas y permutenias desalergenizadas.

2002
- 2002-03-28 CA CA2441562A patent/CA2441562C/en not_active Expired - Lifetime
- 2002-03-28 ES ES09159563T patent/ES2389285T3/es not_active Expired - Lifetime
- 2002-03-28 KR KR1020037012435A patent/KR100891157B1/ko not_active Expired - Lifetime
- 2002-03-28 JP JP2002578411A patent/JP4310107B2/ja not_active Expired - Lifetime
- 2002-03-28 US US10/109,171 patent/US7381704B2/en not_active Expired - Lifetime
- 2002-03-28 EP EP02725386A patent/EP1379265A4/en not_active Withdrawn
- 2002-03-28 WO PCT/US2002/009534 patent/WO2002079408A2/en not_active Ceased
- 2002-03-28 EP EP09159563A patent/EP2105141B1/en not_active Expired - Lifetime
- 2002-03-28 AU AU2002255952A patent/AU2002255952A1/en not_active Abandoned
2009
- 2009-01-13 JP JP2009004309A patent/JP4484941B2/ja not_active Expired - Lifetime

Also Published As

Publication number	Publication date
JP4484941B2 (ja)	2010-06-16
KR100891157B1 (ko)	2009-04-07
KR20040002880A (ko)	2004-01-07
EP1379265A4 (en)	2005-09-14
JP2005506300A (ja)	2005-03-03
US7381704B2 (en)	2008-06-03
EP2105141B1 (en)	2012-08-08
WO2002079408A2 (en)	2002-10-10
EP1379265A2 (en)	2004-01-14
US20030109452A1 (en)	2003-06-12
WO2002079408A3 (en)	2002-11-28
CA2441562C (en)	2013-05-14
AU2002255952A1 (en)	2002-10-15
JP2009137992A (ja)	2009-06-25
EP2105141A1 (en)	2009-09-30
HK1135330A1 (en)	2010-06-04
JP4310107B2 (ja)	2009-08-05
CA2441562A1 (en)	2002-10-10

Publication	Publication Date	Title
ES2389285T3 (es)	2012-10-24	Péptidos bioactivos cortos y procedimientos para su uso
US6875744B2 (en)	2005-04-05	Short bioactive peptides
Leippe et al.	1994	Cytolytic and antibacterial activity of synthetic peptides derived from amoebapore, the pore-forming peptide of Entamoeba histolytica.
Lee et al.	1997	Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate, Styela clava
EP1853620B1 (en)	2012-01-11	Antimicrobial hexapeptides
KR102499670B1 (ko)	2023-02-20	라이신 치환을 포함하는 Romo1 유래 항균 펩타이드 및 그 변이체
US5792831A (en)	1998-08-11	Analogues of magainin peptides containing D-amino acids
JPH08500818A (ja)	1996-01-30	Ｎ末端置換を有する生物活性ペプチド
US5654274A (en)	1997-08-05	Biologically active peptides having N-terminal substitutions
US5217956A (en)	1993-06-08	Composition and treatment with biologically active peptides and certain anions
US20050209157A1 (en)	2005-09-22	Short bioactive peptides and methods for their use
EP1334124B1 (en)	2007-01-03	Diastereomeric peptides and pharmaceutical compositions comprising them
WO2012033450A1 (en)	2012-03-15	Novel antimicrobial peptides
WO1990004408A1 (en)	1990-05-03	Composition and treatment with biologically active peptides and certain anions
WO1991017760A1 (en)	1991-11-28	Composition of and treatment with biologically active peptides having d-amino acid residues
KR101847051B1 (ko)	2018-04-09	병원균에 대한 항생활성을 갖는 펩타이드 및 이를 포함하는 항생 펩타이드 조성물
CA2180748A1 (en)	1995-07-20	Ion-channel forming amphiphilic peptides having n-terminal modifications
HK1135330B (en)	2013-03-22	Short bioactive peptides and methods for their use
KR20220090857A (ko)	2022-06-30	Fk-13 펩타이드를 유효성분으로 포함하는 항균용 화장료 조성물
AU8300598A (en)	1999-02-10	Biologically active peptides with reduced toxicity in animals and a method for preparing same
Rangel et al.	2022	Peptides with Therapeutic Potential against Acinetobacter
Tal et al.	2004	terial peptide that inhibits phagocyte NADPH oxidase activity by binding to Src homology 3 domains of p47 phox. Proceedings of the National Academy of