KR19990071546A - 조정된 프로테그린 - Google Patents
조정된 프로테그린Info
- Publication number
- KR19990071546A KR19990071546A KR1019980703820A KR19980703820A KR19990071546A KR 19990071546 A KR19990071546 A KR 19990071546A KR 1019980703820 A KR1019980703820 A KR 1019980703820A KR 19980703820 A KR19980703820 A KR 19980703820A KR 19990071546 A KR19990071546 A KR 19990071546A
- Authority
- KR
- South Korea
- Prior art keywords
- amino acid
- present
- antimicrobial peptide
- hydrophobic
- basic
- 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.)
- Withdrawn
Links
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- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N63/00—Biocides, pest repellants or attractants, or plant growth regulators containing microorganisms, viruses, microbial fungi, animals or substances produced by, or obtained from, microorganisms, viruses, microbial fungi or animals, e.g. enzymes or fermentates
- A01N63/50—Isolated enzymes; Isolated proteins
-
- 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
- A61K38/10—Peptides having 12 to 20 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Zoology (AREA)
- Epidemiology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biotechnology (AREA)
- Dentistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Communicable Diseases (AREA)
- Agronomy & Crop Science (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Microbiology (AREA)
- Pest Control & Pesticides (AREA)
- Plant Pathology (AREA)
- Virology (AREA)
- Oncology (AREA)
- Wood Science & Technology (AREA)
- Environmental Sciences (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Paints Or Removers (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
Applications Claiming Priority (10)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US56234695A | 1995-11-22 | 1995-11-22 | |
| US8/562,346 | 1995-11-22 | ||
| US64981196A | 1996-05-17 | 1996-05-17 | |
| US8/649,811 | 1996-05-17 | ||
| US69092196A | 1996-08-01 | 1996-08-01 | |
| US690,921 | 1996-08-01 | ||
| US8/690,921 | 1996-08-01 | ||
| US8/752,852 | 1996-11-21 | ||
| US08/752,852 US5994306A (en) | 1995-11-22 | 1996-11-21 | Fine-tuned protegrins |
| PCT/US1996/018544 WO1997018826A1 (en) | 1995-11-22 | 1996-11-22 | Fine tuned protegrins |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| KR19990071546A true KR19990071546A (ko) | 1999-09-27 |
Family
ID=27415886
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1019980703820A Withdrawn KR19990071546A (ko) | 1995-11-22 | 1996-11-22 | 조정된 프로테그린 |
Country Status (12)
| Country | Link |
|---|---|
| US (1) | US5994306A (enExample) |
| EP (1) | EP0862448A4 (enExample) |
| JP (1) | JP2001520639A (enExample) |
| KR (1) | KR19990071546A (enExample) |
| CN (1) | CN1251041A (enExample) |
| AU (1) | AU720467B2 (enExample) |
| BR (1) | BR9611565A (enExample) |
| CZ (1) | CZ159198A3 (enExample) |
| HU (1) | HUP0104431A2 (enExample) |
| NO (2) | NO982311L (enExample) |
| PL (1) | PL336763A1 (enExample) |
| WO (2) | WO1997018826A1 (enExample) |
Families Citing this family (44)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6159936A (en) * | 1993-07-20 | 2000-12-12 | The Regents Of The University Of California | Compositions and methods for treating and preventing microbial and viral infections |
| US6653442B1 (en) | 1993-07-20 | 2003-11-25 | Intrabiotics Pharmaceuticals, Inc. | Protegrins |
| US6307016B1 (en) * | 1995-07-06 | 2001-10-23 | Intrabiotics Pharmaceuticals, Inc. | Parevins and tachytegrins |
| USRE38828E1 (en) * | 1995-07-06 | 2005-10-11 | Intrabiotics Pharmaceuticals, Inc. | Parevins and tachytegrins |
| FR2767323B1 (fr) * | 1997-08-12 | 2001-01-05 | Synt Em | Peptides lineaires derives de peptides antibiotiques, leur preparation et leur utilisation pour vectoriser des substances actives |
| US6043220A (en) * | 1997-12-03 | 2000-03-28 | Intrabiotics Pharmaceuticals, Inc. | Threonine-containing protegrins |
| KR100314721B1 (ko) * | 1998-01-22 | 2001-11-23 | 김일웅 | 생물학적 활성이 있는 신규한 펩타이드 |
| ES2274621T3 (es) * | 1998-03-12 | 2007-05-16 | Georgetown University | Peptidos que contienen una secuencia de reconocimiento del colesterol y usos de los mismos. |
| US7223727B2 (en) | 1998-04-09 | 2007-05-29 | Serono Genetics Institute S.A. | GSSP4 polynucleotides and polypeptides and uses thereof |
| EP0974360A3 (en) * | 1998-06-26 | 2000-03-29 | N.V. Nutricia | Pharmaceutical preparations for use in combatting or preventing surface infections caused by microorganisms |
| NZ509101A (en) * | 1998-06-26 | 2003-07-25 | N | Pharmaceutical preparations for use in combatting or preventing surface infections caused by microorganisms |
| CA2336030A1 (en) * | 1998-07-02 | 2000-01-13 | Stichting Skeletal Tissue Engineering Group Amsterdam | Bone cement with antimicrobial peptides |
| WO2000004915A1 (en) * | 1998-07-23 | 2000-02-03 | Intrabiotics Pharmaceuticals, Inc. | Compositions and methods for the treatment or prevention of pulmonary infections |
| US6335318B1 (en) | 1999-05-10 | 2002-01-01 | The Regents Of The University Of California | Antimicrobial theta defensins and methods of using same |
| EP1252305A2 (en) | 1999-12-08 | 2002-10-30 | Genset | Full-length human cdnas encoding potentially secreted proteins |
| ES2174770T1 (es) * | 1999-12-21 | 2002-11-16 | Innogenetics Nv | Peptidos diseñados para el diagnostico y el tratamiento de artritis reumatoide. |
| BR0001870B1 (pt) * | 2000-05-29 | 2014-02-25 | Peptídeo, processo de obtenção de peptídeo, formulação compreendendo peptídeo, método de prevenção de crescimento de parasitas, fungos e bactérias, método para inativar a endotoxina de bactérias gram-negativas | |
| GB0031425D0 (en) * | 2000-12-22 | 2001-02-07 | Amoebics Ltd | Antibacterial treatments |
| KR100738362B1 (ko) * | 2001-03-19 | 2007-07-12 | 재단법인서울대학교산학협력재단 | 신규한 디아민디티올 유도체 및 그의 방사성 레늄 또는방사성 테크네슘 착체; 그리고, 그의 방사성 레늄 착체와리피오돌을 포함하는 간암 치료용 조성물 및 그의 제조용키트 |
| AU2002317071B2 (en) * | 2001-06-22 | 2008-01-31 | The Hospital For Sick Children | Antimicrobial peptides |
| US7033991B2 (en) | 2001-07-16 | 2006-04-25 | Board Of Supervisors Of Louisiana State University And Agriculture And Mechanical College | Inhibiting furin with polybasic peptides |
| WO2003062266A2 (en) * | 2002-01-22 | 2003-07-31 | Intrabiotics Pharmaceuticals, Inc. | Hybrid synthetic method for antimicrobial peptides |
| WO2003089455A2 (en) | 2002-04-22 | 2003-10-30 | Dow Global Technologies Inc. | Low-cost production of peptides |
| US7119070B2 (en) * | 2002-04-30 | 2006-10-10 | The Regents Of The University Of California | Antimicrobial theta defensins, analogs thereof, and methods of use |
| WO2004005338A1 (en) * | 2002-07-08 | 2004-01-15 | Genova, Ltd. | Secreted peptides |
| US20080255052A1 (en) * | 2004-12-23 | 2008-10-16 | The Regents Of The University Of California | Immunologic regulation by theta defensins |
| US7875620B2 (en) * | 2005-06-30 | 2011-01-25 | Piper Medical, Inc. | Methods of treating microbial infections |
| WO2008030988A2 (en) | 2006-09-06 | 2008-03-13 | The Regents Of The University Of California | Selectively targeted antimicrobial peptides and the use thereof |
| US20090092574A1 (en) | 2006-12-29 | 2009-04-09 | Scott Richard W | Ophthalmic And Otic Compositions Of Facially Amphiphilic Polymers And Oligomers And Uses Thereof |
| KR101430627B1 (ko) | 2008-05-13 | 2014-08-14 | 유니버시티 오브 캔사스 | 금속 추출 펩타이드(map) 태그 및 관련된 방법 |
| TWI394578B (zh) * | 2009-01-09 | 2013-05-01 | Academia Sinica | 抗菌蛋白之新用途 |
| US20100202983A1 (en) * | 2009-02-09 | 2010-08-12 | Jernberg Gary R | Selectively targeted antimicrobials for the treatment of periodontal disease |
| EP2709619B1 (en) | 2011-05-16 | 2017-10-11 | Cellceutix Corporation | Compounds for use in treatment of mucositis |
| US9187735B2 (en) | 2012-06-01 | 2015-11-17 | University Of Kansas | Metal abstraction peptide with superoxide dismutase activity |
| US9925223B2 (en) | 2012-09-25 | 2018-03-27 | Regents Of The University Of Minnesota | Methods for making and using antimicrobial peptides |
| CN103623391B (zh) * | 2013-10-10 | 2014-12-31 | 中山大学 | 抗菌肽Protegrin-1在防治猪蓝耳病中的应用 |
| US20160250298A1 (en) | 2013-11-01 | 2016-09-01 | Spherium Biomed S.L. | Inclusion bodies for transdermal delivery of therapeutic and cosmetic agents |
| CN103936827B (zh) * | 2014-04-22 | 2015-10-14 | 福州大学 | 一种韭菜籽抗菌三肽及其制备方法与应用 |
| CN105175509A (zh) * | 2015-10-19 | 2015-12-23 | 河南科技学院 | 一种抗菌肽xyz-1及其应用 |
| CN108524911B (zh) * | 2018-02-27 | 2022-03-08 | 成都山信药业有限公司 | Protegrin-1抗菌肽衍生物在制备抗口腔致病菌药物中的用途 |
| JP7755994B2 (ja) * | 2018-10-19 | 2025-10-17 | リップタイド バイオサイエンス インコーポレイテッド | 抗菌性ペプチド及びその使用方法 |
| WO2020139852A1 (en) | 2018-12-28 | 2020-07-02 | General Probiotics, Inc. | Combinations of engineered antimicrobial probiotics for treatment of gastrointestinal tract pathogens |
| US11771694B2 (en) | 2020-06-05 | 2023-10-03 | Innovation Pharmaceuticals Inc. | Arylamide compounds for treatment and prevention of viral infections |
| CN113975373A (zh) * | 2021-11-18 | 2022-01-28 | 宁波市眼科医院 | 眼用制剂 |
Family Cites Families (31)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4543252A (en) * | 1982-01-21 | 1985-09-24 | The Regents Of The University Of California | Cationic oligopeptides having microbicidal activity |
| US4652639A (en) * | 1982-05-06 | 1987-03-24 | Amgen | Manufacture and expression of structural genes |
| US4659692A (en) * | 1982-11-19 | 1987-04-21 | The Regents Of The University Of California | Cationic oligopeptides having microbicidal activity |
| US4705777A (en) * | 1985-02-25 | 1987-11-10 | The Regents Of The University Of California | Cationic oligopeptides having microbicidal activity |
| US5338724A (en) * | 1986-11-26 | 1994-08-16 | Cornell Research Foundation, Inc. | Antimicrobial proteins, compositions containing same and uses thereof |
| US5126257A (en) * | 1986-11-26 | 1992-06-30 | Cornell Research Foundation | Antimicrobial proteins, compositions containing same and uses thereof |
| US5087569A (en) * | 1986-11-26 | 1992-02-11 | Cornell Research Foundation, Inc. And The Rockefeller University | Antimicrobial proteins, compositions containing same and uses thereof |
| US5032574A (en) * | 1988-05-26 | 1991-07-16 | Invitron Corporation | Novel antimicrobial peptide |
| US5171739A (en) * | 1989-02-14 | 1992-12-15 | Incyte Pharmaceuticals, Inc. | Treatment of endotoxin-associated shock and preventation thereof using a BPI protein |
| US5308834A (en) * | 1989-02-14 | 1994-05-03 | Incyte Pharmaceuticals, Inc. | Treatment of endotoxin-associated shock and prevention thereof using a BPI protein |
| US5234912A (en) * | 1989-02-14 | 1993-08-10 | Incyte Pharmaceuticals, Inc. | Pharmaceutical compositions comprising recombinant BPI proteins and a lipid carrier and uses thereof |
| US5334584A (en) * | 1989-02-14 | 1994-08-02 | Incyte Pharamaceuticals, Inc. | Recombinant, non-glycosylated bpi protein and uses thereof |
| US5102870A (en) * | 1989-04-14 | 1992-04-07 | Schering Ag | Treatment and prevention of oral mucositis with growth factors |
| US5484885A (en) * | 1989-07-05 | 1996-01-16 | Emory University | Chemotactic, antibiotic and lipopolysaccharide-binding peptide fragments of CAP37 |
| US5607916A (en) * | 1989-07-05 | 1997-03-04 | The Board Of Regents Of The University Of Oklahoma | Method and composition for the treatment of septic shock |
| US5447914A (en) * | 1990-06-21 | 1995-09-05 | Emory University | Antimicrobial peptides |
| US5432270A (en) * | 1990-10-25 | 1995-07-11 | Zasloff; Michael A. | DNA encoding tracheal antimicrobial peptides |
| AU667479B2 (en) * | 1991-06-12 | 1996-03-28 | Magainin Pharmaceuticals, Inc. | Treating the oral cavity with ion-channel forming peptides |
| US5488035A (en) * | 1991-12-06 | 1996-01-30 | Pioneer Hi-Bred International, Inc. | Peptide with inhibitory activity towards plant pathogenic fungi |
| AU678362B2 (en) * | 1992-05-26 | 1997-05-29 | General Hospital Corporation, The | Antibiotic cryptdin peptides and methods of their use |
| JPH08504085A (ja) * | 1992-07-17 | 1996-05-07 | パノラマ リサーチ,インコーポレイティド | リポ多糖体結合及び抗擬血活性をもつ哺乳動物のカチオン性タンパク質 |
| US5459235A (en) * | 1993-03-19 | 1995-10-17 | The Regents Of The University Of California | Antimicrobial peptides antibodies and nucleic acid molecules from bovine neutrophils |
| AU7050294A (en) * | 1993-06-04 | 1995-01-03 | Demeter Biotechnologies, Ltd. | Method of treating pulmonary disease states with non-naturally occurring amphipathic peptides |
| US5464823A (en) * | 1993-07-20 | 1995-11-07 | The Regents Of The University Of California | Mammalian antibiotic peptides |
| US5693486A (en) * | 1993-07-20 | 1997-12-02 | Intrabiotics | DNA sequences encoding protegrins and protegrin analogs and their use in recombinant methods of producing protegrins |
| US5804558A (en) * | 1993-07-20 | 1998-09-08 | University Of California | Protegrins |
| US5708145A (en) * | 1993-07-20 | 1998-01-13 | University Of California | Immunglobulins reactive with protegrins |
| EP0677061B1 (en) * | 1993-10-14 | 1999-03-03 | Seikagaku Corporation | Polypeptides and anti-hiv agents prepared therefrom |
| US5804553A (en) * | 1994-04-05 | 1998-09-08 | University Of California | Prophenins - antibiotic peptides |
| US5589364A (en) * | 1994-07-29 | 1996-12-31 | Magainin Pharmaceuticals Inc. | Recombinant production of biologically active peptides and proteins |
| CA2226121A1 (en) * | 1995-07-06 | 1997-01-23 | Intrabiotics Pharmaceuticals, Incorporated | Parevins and tachytegrins |
-
1996
- 1996-11-21 US US08/752,852 patent/US5994306A/en not_active Expired - Lifetime
- 1996-11-22 JP JP51984797A patent/JP2001520639A/ja not_active Ceased
- 1996-11-22 WO PCT/US1996/018544 patent/WO1997018826A1/en not_active Ceased
- 1996-11-22 AU AU77394/96A patent/AU720467B2/en not_active Ceased
- 1996-11-22 WO PCT/US1996/018845 patent/WO1997018827A1/en not_active Ceased
- 1996-11-22 HU HU0104431A patent/HUP0104431A2/hu unknown
- 1996-11-22 PL PL96336763A patent/PL336763A1/xx unknown
- 1996-11-22 CZ CZ981591A patent/CZ159198A3/cs unknown
- 1996-11-22 CN CN96199632A patent/CN1251041A/zh active Pending
- 1996-11-22 EP EP96940535A patent/EP0862448A4/en not_active Withdrawn
- 1996-11-22 BR BR9611565-3A patent/BR9611565A/pt not_active Application Discontinuation
- 1996-11-22 KR KR1019980703820A patent/KR19990071546A/ko not_active Withdrawn
-
1998
- 1998-05-20 NO NO982311A patent/NO982311L/no unknown
- 1998-05-20 NO NO982310A patent/NO982310L/no unknown
Also Published As
| Publication number | Publication date |
|---|---|
| AU7739496A (en) | 1997-06-11 |
| HUP0104431A2 (hu) | 2002-03-28 |
| PL336763A1 (en) | 2000-07-17 |
| NO982310D0 (no) | 1998-05-20 |
| EP0862448A4 (en) | 1999-03-31 |
| US5994306A (en) | 1999-11-30 |
| BR9611565A (pt) | 1999-12-28 |
| AU720467B2 (en) | 2000-06-01 |
| NO982311L (no) | 1998-07-22 |
| EP0862448A1 (en) | 1998-09-09 |
| JP2001520639A (ja) | 2001-10-30 |
| CN1251041A (zh) | 2000-04-19 |
| NO982310L (no) | 1998-07-22 |
| NO982311D0 (no) | 1998-05-20 |
| WO1997018827A1 (en) | 1997-05-29 |
| WO1997018826A1 (en) | 1997-05-29 |
| CZ159198A3 (cs) | 1998-10-14 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PA0105 | International application |
Patent event date: 19980522 Patent event code: PA01051R01D Comment text: International Patent Application |
|
| PG1501 | Laying open of application | ||
| PC1203 | Withdrawal of no request for examination | ||
| WITN | Application deemed withdrawn, e.g. because no request for examination was filed or no examination fee was paid |