MX2011000975A - Analogos de peptido b amiloide, oligomeros de los mismos, procedimientos para preparar y composiciones que comprenden dichos analogos u oligomeros, y sus usos. - Google Patents
Analogos de peptido b amiloide, oligomeros de los mismos, procedimientos para preparar y composiciones que comprenden dichos analogos u oligomeros, y sus usos.Info
- Publication number
- MX2011000975A MX2011000975A MX2011000975A MX2011000975A MX2011000975A MX 2011000975 A MX2011000975 A MX 2011000975A MX 2011000975 A MX2011000975 A MX 2011000975A MX 2011000975 A MX2011000975 A MX 2011000975A MX 2011000975 A MX2011000975 A MX 2011000975A
- Authority
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- Mexico
- Prior art keywords
- amino acid
- acid residue
- sequence
- covalently linked
- amyloid peptide
- Prior art date
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Classifications
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- 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
- C07K14/4711—Alzheimer's disease; Amyloid plaque core protein
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- 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
-
- 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
-
- 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
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/46—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans from vertebrates
- G01N2333/47—Assays involving proteins of known structure or function as defined in the subgroups
- G01N2333/4701—Details
- G01N2333/4709—Amyloid plaque core protein
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2500/00—Screening for compounds of potential therapeutic value
- G01N2500/04—Screening involving studying the effect of compounds C directly on molecule A (e.g. C are potential ligands for a receptor A, or potential substrates for an enzyme A)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
- G01N2800/2814—Dementia; Cognitive disorders
- G01N2800/2821—Alzheimer
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Neurology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Toxicology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Immunology (AREA)
- Neurosurgery (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Psychiatry (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Hospice & Palliative Care (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US8358908P | 2008-07-25 | 2008-07-25 | |
| PCT/US2009/051721 WO2010011947A2 (en) | 2008-07-25 | 2009-07-24 | AMYLOID ß PEPTIDE ANALOGUES, OLIGOMERS THEREOF, PROCESSES FOR PREPARING AND COMPOSITIONS COMPRISING SAID ANALOGUES OR OLIGOMERS, AND THEIR USES |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MX2011000975A true MX2011000975A (es) | 2011-05-25 |
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ID=41570887
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MX2011000975A MX2011000975A (es) | 2008-07-25 | 2009-07-24 | Analogos de peptido b amiloide, oligomeros de los mismos, procedimientos para preparar y composiciones que comprenden dichos analogos u oligomeros, y sus usos. |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US20110092445A1 (cg-RX-API-DMAC7.html) |
| EP (1) | EP2303920A4 (cg-RX-API-DMAC7.html) |
| JP (1) | JP2011529084A (cg-RX-API-DMAC7.html) |
| CN (1) | CN102203124A (cg-RX-API-DMAC7.html) |
| CA (1) | CA2730804A1 (cg-RX-API-DMAC7.html) |
| MX (1) | MX2011000975A (cg-RX-API-DMAC7.html) |
| WO (1) | WO2010011947A2 (cg-RX-API-DMAC7.html) |
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| DE10303974A1 (de) | 2003-01-31 | 2004-08-05 | Abbott Gmbh & Co. Kg | Amyloid-β(1-42)-Oligomere, Verfahren zu deren Herstellung und deren Verwendung |
| PT1954718E (pt) | 2005-11-30 | 2014-12-16 | Abbvie Inc | Anticorpos anti-globulómeros aβ, suas porções de ligação ao antigénio, correspondentes hibridomas, ácidos nucleicos, vectores, células hospedeiras, métodos de produção dos ditos anticorpos, composições compreendendo os ditos anticorpos, usos dos ditos anticorpos e métodos para uso dos ditos anticorpos |
| PL1976877T5 (pl) | 2005-11-30 | 2017-09-29 | Abbvie Inc | Przeciwciała monoklonalne przeciwko białku amyloidu beta oraz ich zastosowania |
| US8455626B2 (en) | 2006-11-30 | 2013-06-04 | Abbott Laboratories | Aβ conformer selective anti-aβ globulomer monoclonal antibodies |
| US20100311767A1 (en) | 2007-02-27 | 2010-12-09 | Abbott Gmbh & Co. Kg | Method for the treatment of amyloidoses |
| EP2262526B1 (en) * | 2008-04-14 | 2015-12-02 | Alzinova AB | Stable amyloid beta monomers and oligomers |
| AU2009266552B2 (en) * | 2008-07-01 | 2014-01-23 | De Staat Der Nederlanden, Vert. Door De Minister Van Vws | Vaccine against amyloid folding intermediate |
| US8486940B2 (en) | 2009-09-11 | 2013-07-16 | Probiodrug Ag | Inhibitors |
| MX341536B (es) * | 2010-03-03 | 2016-08-24 | The Univ Of British Columbia * | Epitopo y anticuerpos beta amiloide de oligomero especifico. |
| AU2013205000B2 (en) * | 2010-03-03 | 2015-05-28 | The University Of British Columbia | Oligomer-specific amyloid beta epitope and antibodies |
| CN102933601B (zh) | 2010-04-15 | 2016-06-08 | Abbvie公司 | β淀粉样蛋白结合蛋白 |
| US9364449B2 (en) | 2010-06-09 | 2016-06-14 | New York University | Peptoid and synthetic oligomers, pharmaceutical compositions and methods of using same |
| MX358739B (es) | 2010-08-14 | 2018-09-03 | Abbvie Inc Star | Proteinas de union a amiloide beta. |
| US20120089291A1 (en) * | 2010-10-12 | 2012-04-12 | Halder Bibhrajit | Autonomous machine control system |
| US11231426B2 (en) | 2010-11-29 | 2022-01-25 | Inven2 As | Methods and compositions for monitoring phagocytic activity |
| WO2012072611A1 (de) * | 2010-11-29 | 2012-06-07 | Philipps-Universität Marburg | SYNTHETISCHE LIGANDEN FÜR HUMANE ANTI-Aβ-ANTIKÖRPER |
| JP6220344B2 (ja) * | 2011-11-29 | 2017-10-25 | プロクララ バイオサイエンシーズ， インコーポレイテッド | アミロイド結合剤としてのバクテリオファージのｐ３の使用 |
| US20130164217A1 (en) * | 2011-12-21 | 2013-06-27 | Meso Scale Technologies, Llc | Method of diagnosing, preventing and/or treating dementia & related disorders |
| DE102012021222B4 (de) * | 2012-10-27 | 2015-02-05 | Forschungszentrum Jülich GmbH | Verfahren zur Herstellung einer nanoporösen Schicht auf einem Substrat |
| EP2746402A1 (en) * | 2013-03-12 | 2014-06-25 | Academisch Medisch Centrum | Method of prognosis of Alzheimers disease and substrates for use therein |
| EP2787349A1 (en) | 2013-04-03 | 2014-10-08 | Affiris AG | Method for detecting proteinopathy-specific antibodies in a biological sample |
| EP2787347A1 (en) * | 2013-04-03 | 2014-10-08 | Affiris AG | Method for detecting Aß-specific antibodies in a biological sample |
| KR102331422B1 (ko) | 2014-01-31 | 2021-11-25 | 카그니션 테라퓨틱스, 인코퍼레이티드 | 아이소인돌린 조성물 및 신경퇴행성 질환을 치료하는 방법 |
| EP3166969A2 (en) * | 2014-07-07 | 2017-05-17 | AbbVie Deutschland GmbH & Co. KG | IMMUNOGENIC PRODUCTS BASED ON MUTEIN AMYLOID ß (Aß) AMINO ACID SEQUENCES AND USES THEREOF |
| JP6675403B2 (ja) * | 2014-09-05 | 2020-04-01 | システム オブ システムズ アナリティクス インコーポレイテッド | アミロイドベータオリゴマーを検出する方法 |
| ES2571055B1 (es) * | 2016-02-15 | 2016-12-28 | Araclon Biotech, S.L. | Conjugado amiloide y usos y procedimientos del mismo |
| WO2018005980A1 (en) * | 2016-07-01 | 2018-01-04 | The Scripps Research Institute | Compositions and diagnostic methods related to transthyretin amyloid diseases |
| US11214540B2 (en) | 2017-05-15 | 2022-01-04 | Cognition Therapeutics, Inc. | Compositions for treating neurodegenerative diseases |
| PL3461819T3 (pl) | 2017-09-29 | 2020-11-30 | Probiodrug Ag | Inhibitory cyklazy glutaminylowej |
| CN108148115A (zh) * | 2018-01-30 | 2018-06-12 | 中国药科大学 | 一种环肽合成新方法及其在药物开发中的应用 |
| US20210262006A1 (en) * | 2018-06-18 | 2021-08-26 | Emory University | Parallel Enzyme Digestion for Protein Biomarker Detection |
| CN109912687A (zh) * | 2019-03-20 | 2019-06-21 | 横琴欣健生物科技研究院有限公司 | 一种治疗老年痴呆症的多肽药物 |
| CN109851660A (zh) * | 2019-03-20 | 2019-06-07 | 横琴欣健生物科技研究院有限公司 | 一种治疗老年痴呆症的多肽及其疫苗 |
| JP7357354B2 (ja) * | 2020-02-04 | 2023-10-06 | 国立大学法人京都大学 | アミロイドβ４２架橋アナログペプチド |
| KR102767892B1 (ko) * | 2021-12-30 | 2025-02-14 | 고려대학교 산학협력단 | 신규한 단백질 변이체 및 이를 이용한 신경퇴행성 질환 치료용 조성물 |
| US12037375B2 (en) * | 2021-12-30 | 2024-07-16 | Korea University Research And Business Foundation | Protein variant and composition for treating neurodegenerative disease using the same |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5750349A (en) * | 1993-01-25 | 1998-05-12 | Takeda Chemical Industries Ltd. | Antibodies to β-amyloids or their derivatives and use thereof |
| DE10101430B4 (de) * | 2001-01-13 | 2008-10-02 | Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. | Lösliche cyclische Analoga zur Modulation der Amyloidogenese |
| US20020132758A1 (en) * | 2001-01-18 | 2002-09-19 | Shell John W. | Method for identifying compounds to treat medical pathologies associated with molecular crystallization |
| US20070213512A1 (en) * | 2002-10-01 | 2007-09-13 | Krafft Grant A | Amyloid beta peptide analogs and assemblies thereof |
| DE10303974A1 (de) * | 2003-01-31 | 2004-08-05 | Abbott Gmbh & Co. Kg | Amyloid-β(1-42)-Oligomere, Verfahren zu deren Herstellung und deren Verwendung |
| EP1676859A1 (en) * | 2004-12-30 | 2006-07-05 | Pevion Biotech Ltd. | Immunogenic compositions of cyclic peptides derived from the beta-amyloid peptide |
| CN101365717A (zh) * | 2005-03-05 | 2009-02-11 | 艾博特股份有限两合公司 | 筛选方法、纯化非扩散A-β寡聚体的方法、抗所述非扩散A-β寡聚体的选择性抗体以及制备所述抗体的方法 |
| WO2007064917A2 (en) * | 2005-11-30 | 2007-06-07 | Abbott Laboratories | Methods of preparation of recombinant forms of human beta-amyloid protein and uses of these proteins |
| DK2091948T3 (da) * | 2006-11-30 | 2012-07-23 | Probiodrug Ag | Nye inhibitorer af glutaminylcyclase |
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- 2009-07-24 CA CA2730804A patent/CA2730804A1/en not_active Abandoned
- 2009-07-24 US US12/509,325 patent/US20110092445A1/en not_active Abandoned
- 2009-07-24 EP EP09801088A patent/EP2303920A4/en not_active Withdrawn
- 2009-07-24 MX MX2011000975A patent/MX2011000975A/es not_active Application Discontinuation
- 2009-07-24 WO PCT/US2009/051721 patent/WO2010011947A2/en not_active Ceased
- 2009-07-24 JP JP2011520233A patent/JP2011529084A/ja active Pending
- 2009-07-24 CN CN200980137576XA patent/CN102203124A/zh active Pending
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| WO2010011947A2 (en) | 2010-01-28 |
| US20110092445A1 (en) | 2011-04-21 |
| EP2303920A4 (en) | 2011-11-09 |
| CN102203124A (zh) | 2011-09-28 |
| EP2303920A2 (en) | 2011-04-06 |
| CA2730804A1 (en) | 2010-01-28 |
| WO2010011947A3 (en) | 2010-04-29 |
| JP2011529084A (ja) | 2011-12-01 |
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