CA2969128A1 - Polypeptides comprising a modified bacteriophage g3p amino acid sequence lacking a glycosylation signal - Google Patents
Polypeptides comprising a modified bacteriophage g3p amino acid sequence lacking a glycosylation signal Download PDFInfo
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- CA2969128A1 CA2969128A1 CA2969128A CA2969128A CA2969128A1 CA 2969128 A1 CA2969128 A1 CA 2969128A1 CA 2969128 A CA2969128 A CA 2969128A CA 2969128 A CA2969128 A CA 2969128A CA 2969128 A1 CA2969128 A1 CA 2969128A1
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- A61P25/00—Drugs for disorders of the nervous system
- A61P25/28—Drugs for disorders of the nervous system for treating neurodegenerative disorders of the central nervous system, e.g. nootropic agents, cognition enhancers, drugs for treating Alzheimer's disease or other forms of dementia
-
- 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
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
-
- 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
- C12N2795/00—Bacteriophages
- C12N2795/00011—Details
- C12N2795/14011—Details ssDNA Bacteriophages
- C12N2795/14022—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Neurology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Biomedical Technology (AREA)
- Neurosurgery (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Epidemiology (AREA)
- Virology (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Marine Sciences & Fisheries (AREA)
- Zoology (AREA)
- Psychology (AREA)
- Dermatology (AREA)
- Psychiatry (AREA)
- Hospice & Palliative Care (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Physical Education & Sports Medicine (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201462087052P | 2014-12-03 | 2014-12-03 | |
| US62/087,052 | 2014-12-03 | ||
| PCT/US2015/063476 WO2016090022A1 (en) | 2014-12-03 | 2015-12-02 | Polypeptides comprising a modified bacteriophage g3p amino acid sequence lacking a gylcosylation signal |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2969128A1 true CA2969128A1 (en) | 2016-06-09 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2969128A Abandoned CA2969128A1 (en) | 2014-12-03 | 2015-12-02 | Polypeptides comprising a modified bacteriophage g3p amino acid sequence lacking a glycosylation signal |
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| US (2) | US10722551B2 (enExample) |
| EP (1) | EP3227313B1 (enExample) |
| JP (2) | JP6730988B2 (enExample) |
| KR (1) | KR20170085132A (enExample) |
| CN (1) | CN107250154A (enExample) |
| AR (1) | AR102890A1 (enExample) |
| AU (1) | AU2015358504A1 (enExample) |
| BR (1) | BR112017011530A2 (enExample) |
| CA (1) | CA2969128A1 (enExample) |
| DK (1) | DK3227313T3 (enExample) |
| EA (1) | EA201791212A1 (enExample) |
| ES (1) | ES2910017T3 (enExample) |
| IL (1) | IL252426A0 (enExample) |
| MX (1) | MX2017007059A (enExample) |
| PH (1) | PH12017501004A1 (enExample) |
| PL (1) | PL3227313T3 (enExample) |
| PT (1) | PT3227313T (enExample) |
| SG (1) | SG11201704427YA (enExample) |
| TW (1) | TW201632542A (enExample) |
| WO (1) | WO2016090022A1 (enExample) |
Families Citing this family (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2785364B1 (en) | 2011-11-29 | 2019-01-09 | Proclara Biosciences, Inc. | Use of p3 of bacteriophage as amyloid binding agents |
| MX358755B (es) | 2012-10-02 | 2018-09-03 | Proclara Biosciences Inc | Uso del p3 de proteinas de fusion de bacteriofago como agentes de union amiloides. |
| US9988444B2 (en) | 2013-05-28 | 2018-06-05 | Proclara Biosciences, Inc. | Polypeptides comprising a modified bacteriophage g3p amino acid sequence with reduced immunogenicity |
| SG11201704427YA (en) | 2014-12-03 | 2017-06-29 | Proclara Biosciences Inc | Polypeptides comprising a modified bacteriophage g3p amino acid sequence lacking a gylcosylation signal |
| US11692017B2 (en) | 2018-06-15 | 2023-07-04 | Amyl Therapeutics Srl | General amyloid interaction motif (GAIM) |
| KR20250110352A (ko) | 2022-12-02 | 2025-07-18 | 알제온, 인크. | 트라미프로세이트를 이용하여 신경퇴행성 장애를 치료하는 방법 |
Family Cites Families (32)
| Publication number | Priority date | Publication date | Assignee | Title |
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| US3941763A (en) | 1975-03-28 | 1976-03-02 | American Home Products Corporation | PGlu-D-Met-Trp-Ser-Tyr-D-Ala-Leu-Arg-Pro-Gly-NH2 and intermediates |
| US4215051A (en) | 1979-08-29 | 1980-07-29 | Standard Oil Company (Indiana) | Formation, purification and recovery of phthalic anhydride |
| EP0154316B1 (en) | 1984-03-06 | 1989-09-13 | Takeda Chemical Industries, Ltd. | Chemically modified lymphokine and production thereof |
| EP0401384B1 (en) | 1988-12-22 | 1996-03-13 | Kirin-Amgen, Inc. | Chemically modified granulocyte colony stimulating factor |
| DE10399023I2 (de) | 1989-09-12 | 2006-11-23 | Ahp Mfg B V | TFN-bindende Proteine |
| US6552170B1 (en) | 1990-04-06 | 2003-04-22 | Amgen Inc. | PEGylation reagents and compounds formed therewith |
| US5252714A (en) | 1990-11-28 | 1993-10-12 | The University Of Alabama In Huntsville | Preparation and use of polyethylene glycol propionaldehyde |
| ES2199935T3 (es) | 1991-03-15 | 2004-03-01 | Amgen Inc. | Pegilacion de polipeptidos. |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| WO1993024135A1 (en) | 1992-05-26 | 1993-12-09 | Immunex Corporation | Novel cytokine that binds cd30 |
| ES2258817T3 (es) | 1997-05-21 | 2006-09-01 | Biovation Limited | Metodo para la produccion de proteinas no inmunogenas. |
| ATE352559T1 (de) | 1998-12-08 | 2007-02-15 | Biovation Ltd | Verfahren zur verminderung der immunogenität von proteinen |
| US20020052311A1 (en) | 1999-09-03 | 2002-05-02 | Beka Solomon | Methods and compostions for the treatment and/or diagnosis of neurological diseases and disorders |
| US8022270B2 (en) | 2000-07-31 | 2011-09-20 | Biolex Therapeutics, Inc. | Expression of biologically active polypeptides in duckweed |
| AU2002233340B2 (en) | 2001-02-19 | 2008-05-22 | Merck Patent Gmbh | Artificial fusion proteins with reduced immunogenicity |
| KR20030082962A (ko) | 2001-03-08 | 2003-10-23 | 메르크 파텐트 게엠베하 | 감소된 면역원성을 갖는 개질된과립구대식세포집락자극인자(gm-csf) |
| DE10238846A1 (de) | 2002-08-20 | 2004-03-04 | Nemod Immuntherapie Ag | Aktive Fusionsproteine und Verfahren zu ihrer Herstellung |
| JP5096169B2 (ja) | 2005-02-01 | 2012-12-12 | ラモット・アット・テルアビブ・ユニバーシティ | アミロイド沈着に付随する炎症および活性化されたマイクログリアにかかわる脳の炎症の処置法 |
| AU2007214399A1 (en) | 2006-02-15 | 2007-08-23 | Ramot At Tel-Aviv University | Filamentous bacteriophage displaying protein as a binder of antibodies and immunocomplexes for delivery to the brain |
| WO2007094003A2 (en) | 2006-02-15 | 2007-08-23 | Ramot At Tel Aviv University Ltd. | Viral display vehicles for treating multiple sclerosis |
| WO2007109733A2 (en) | 2006-03-21 | 2007-09-27 | The Johns Hopkins University | Diagnostic and prognostic markers and treatment strategies for multiple sclerosis |
| US20090105090A1 (en) | 2006-04-06 | 2009-04-23 | Fumiaki Uchiyama | Phage Display By Novel Filamentous Bacteriophage |
| CN101553567A (zh) | 2006-07-21 | 2009-10-07 | 台拉维夫大学拉莫特 | 抑制或治疗与细胞内形成蛋白纤维状内含体或聚集体相关的疾病的方法 |
| KR101485202B1 (ko) | 2006-10-11 | 2015-01-22 | 안티토페 리미티드 | T 세포 에피토프 데이터베이스들 |
| WO2009143470A1 (en) | 2008-05-22 | 2009-11-26 | Ramot At Tel Aviv University Ltd. | Method for treating disease characterized by plaque |
| AU2009316326A1 (en) | 2008-11-24 | 2010-05-27 | Ramot At Tel-Aviv University Ltd. | Method for treating Parkinson' s disease using filamentous bacteriophage |
| WO2011084714A2 (en) | 2009-12-17 | 2011-07-14 | Biogen Idec Ma Inc. | STABILIZED ANTI-TNF-ALPHA scFv MOLECULES OR ANTI-TWEAK scFv MOLECULES AND USES THEREOF |
| JP2014509514A (ja) | 2011-03-11 | 2014-04-21 | ラモット アット テルアヴィブ ユニヴァーシティ リミテッド | 神経変性タウオパシーを治療するための方法 |
| EP2785364B1 (en) * | 2011-11-29 | 2019-01-09 | Proclara Biosciences, Inc. | Use of p3 of bacteriophage as amyloid binding agents |
| MX358755B (es) | 2012-10-02 | 2018-09-03 | Proclara Biosciences Inc | Uso del p3 de proteinas de fusion de bacteriofago como agentes de union amiloides. |
| US9988444B2 (en) * | 2013-05-28 | 2018-06-05 | Proclara Biosciences, Inc. | Polypeptides comprising a modified bacteriophage g3p amino acid sequence with reduced immunogenicity |
| SG11201704427YA (en) | 2014-12-03 | 2017-06-29 | Proclara Biosciences Inc | Polypeptides comprising a modified bacteriophage g3p amino acid sequence lacking a gylcosylation signal |
-
2015
- 2015-12-02 SG SG11201704427YA patent/SG11201704427YA/en unknown
- 2015-12-02 CN CN201580065696.9A patent/CN107250154A/zh active Pending
- 2015-12-02 MX MX2017007059A patent/MX2017007059A/es unknown
- 2015-12-02 WO PCT/US2015/063476 patent/WO2016090022A1/en not_active Ceased
- 2015-12-02 TW TW104140347A patent/TW201632542A/zh unknown
- 2015-12-02 PT PT158310110T patent/PT3227313T/pt unknown
- 2015-12-02 KR KR1020177017763A patent/KR20170085132A/ko not_active Withdrawn
- 2015-12-02 CA CA2969128A patent/CA2969128A1/en not_active Abandoned
- 2015-12-02 BR BR112017011530A patent/BR112017011530A2/pt not_active Application Discontinuation
- 2015-12-02 EP EP15831011.0A patent/EP3227313B1/en active Active
- 2015-12-02 JP JP2017529043A patent/JP6730988B2/ja active Active
- 2015-12-02 EA EA201791212A patent/EA201791212A1/ru unknown
- 2015-12-02 PL PL15831011T patent/PL3227313T3/pl unknown
- 2015-12-02 ES ES15831011T patent/ES2910017T3/es active Active
- 2015-12-02 AU AU2015358504A patent/AU2015358504A1/en not_active Abandoned
- 2015-12-02 DK DK15831011.0T patent/DK3227313T3/da active
- 2015-12-02 US US15/532,820 patent/US10722551B2/en active Active
- 2015-12-03 AR ARP150103956A patent/AR102890A1/es unknown
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2017
- 2017-05-22 IL IL252426A patent/IL252426A0/en unknown
- 2017-05-31 PH PH12017501004A patent/PH12017501004A1/en unknown
-
2020
- 2020-02-19 JP JP2020026300A patent/JP2020073610A/ja not_active Withdrawn
- 2020-06-18 US US16/905,128 patent/US11723951B2/en active Active
Also Published As
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| AR102890A1 (es) | 2017-03-29 |
| PH12017501004A1 (en) | 2017-12-18 |
| JP2020073610A (ja) | 2020-05-14 |
| ES2910017T3 (es) | 2022-05-11 |
| US20180207231A1 (en) | 2018-07-26 |
| EP3227313B1 (en) | 2022-02-09 |
| JP6730988B2 (ja) | 2020-07-29 |
| US11723951B2 (en) | 2023-08-15 |
| DK3227313T3 (da) | 2022-04-19 |
| BR112017011530A2 (pt) | 2018-03-13 |
| WO2016090022A1 (en) | 2016-06-09 |
| PL3227313T3 (pl) | 2022-05-09 |
| EA201791212A1 (ru) | 2018-01-31 |
| AU2015358504A1 (en) | 2017-06-29 |
| US20210015895A1 (en) | 2021-01-21 |
| AU2015358504A8 (en) | 2017-07-13 |
| IL252426A0 (en) | 2017-07-31 |
| SG11201704427YA (en) | 2017-06-29 |
| JP2017538407A (ja) | 2017-12-28 |
| TW201632542A (zh) | 2016-09-16 |
| KR20170085132A (ko) | 2017-07-21 |
| US10722551B2 (en) | 2020-07-28 |
| MX2017007059A (es) | 2018-05-02 |
| WO2016090022A8 (en) | 2017-06-22 |
| WO2016090022A9 (en) | 2016-08-25 |
| CN107250154A (zh) | 2017-10-13 |
| PT3227313T (pt) | 2022-04-12 |
| EP3227313A1 (en) | 2017-10-11 |
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