FIBER DIFFRACTION FROM AMYLOID FILAMENTS

淀粉样蛋白丝的纤维衍射

• 批准号: 7601776
• 负责人: GERALD J STUBBS
• 金额: $ 2.06万
• 依托单位: ILLINOIS INSTITUTE OF TECHNOLOGY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-04-01 至 2008-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7601776
• 关键词: Alzheimer' s Disease; Amyloid; Amyloid Proteins; Amyloidosis; Bovine Spongiform Encephalopathy; Cessation of life; Computer Retrieval of Information on Scientific Projects Database; Condition; Crystallography; Data; Drug Design; Electron Microscopy; Fiber; Filament; Funding; Grant; Institution; Methods; Molecular Conformation; Preparation; Prion Diseases; Prions; Proteins; Research; Research Personnel; Resources; Source; Specimen; Structure; United States National Institutes of Health; amyloid formation; improved; insoluble fiber; magnetic field; protein folding; synchrotron radiation

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Amyloids are formed when proteins change conformation to form insoluble fibers that can cause severe damage and death. Amyloidoses include Alzheimers disease and a variety of prion diseases including Creutzfeldt-Jakob and BSE (mad cow disease). Mammalian prions are formed by the protein PrP. Amyloid proteins share a cross-beta structure, but have resisted characterization by crystallography and NMR. Fiber diffraction, in combination with electron microscopy, offers the best hope for structure determination. Structural studies are needed to answer fundamental protein folding questions, to understand amyloid formation, and for rational drug design. We use oriented sols and dried fibers made in high magnetic fields under controlled conditions. Improved prion availability, improved methods of specimen preparation, and synchrotron radiation offer unprecedented opportunities to obtain improved amyloid diffraction data.

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 当蛋白质改变构象形成不溶纤维时，就会形成淀粉样蛋白，这可能会导致严重的损害和死亡。淀粉样变性包括阿尔茨海默病和多种普恩病毒病，包括克雅氏病和疯牛病。哺乳动物的Prion是由PrP蛋白形成的。淀粉样蛋白具有交叉β结构，但不能通过结晶学和核磁共振进行表征。纤维衍射与电子显微镜相结合，为结构测定提供了最大的希望。需要结构研究来回答基本的蛋白质折叠问题，了解淀粉样蛋白的形成，并进行合理的药物设计。 我们使用定向溶胶和在强磁场中在受控条件下制成的干纤维。Prion可用性的提高、样品制备方法的改进以及同步辐射为获得改进的淀粉样衍射数据提供了前所未有的机会。