Identification of peptide epimers in crystallin proteins

晶状体蛋白中肽差向异构体的鉴定

• 批准号: 8901229
• 负责人: Ryan Roy Julian
• 金额: $ 26.75万
• 依托单位: UNIVERSITY OF CALIFORNIA RIVERSIDE
• 依托单位国家: 美国
• 财政年份: 2014
• 资助国家: 美国
• 起止时间: 2014-08-01 至 2018-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8901229
• 关键词: Acids; Affect; Age; Age-Years; Aging; Alzheimer' s Disease; Amino Acids; Aspartic Acid; Automation; Blindness; Cataract; Collagen; Crystallins; Cysteine; Data Analyses; Dentin; Development; Disease; Dissociation; Eye Lens Protein; Funding; Generic Drugs; Goals; Handedness; Health; Human; Individual; Isoaspartic Acid; Isomerism; Lead; Life; Manuals; Mass Spectrum Analysis; Methods; Modification; Molecular; Molecular Chaperones; Motivation; Myopathy; Outcome; Oxidative Stress; Pathology; Peptides; Performance; Play; Post-Translational Protein Processing; Proteins; Proteomics; Protocols documentation; Research; Resolution; Role; Sampling; Site; Structure; Techniques; United States National Institutes of Health; Work; base; cost; disulfide bond; epimerization; extreme temperature; improved; innovation; insight; instrument; interest; lens; mass spectrometer; migration; prevent; programs; protein aggregation; protein degradation; protein structure; racemization; research study; scale up; tool

DESCRIPTION (provided by applicant): The overall goal of this project is to employ an innovative mass spectrometric technique to detect and characterize modifications to the chirality of individual amino acids within peptides and proteins. Chirality, or the handedness of a molecule, is a crucial attribute that influences both structure and function. Changes in chirality are very difficult to detect; however, a new method dependent on site specific radical migration is extremely sensitive to structure and can detect changes in chirality. The underlying motivation for performing this research is to investigate potential causes of cataract disease and to understand how protein modifications influence aging in general. Changes in chirality have been examined in primarily a generic sense in eye lens proteins previously, and these changes have been noted to increase for cataractous lenses. Site-specific examination of changes in chirality has not been carried out previously because no suitable tool was available for performing the task. The outcome of this project will be detailed information that elucidates how chiral inversion contributes to cataract formation and to aging in general, which is necessary to guide the development of potential preventative treatments.

描述（由申请人提供）：该项目的总体目标是采用创新的质谱技术来检测和表征肽和蛋白质中单个氨基酸的手性修饰。手性，或分子的手性，是影响结构和功能的关键属性。手性的变化很难检测；然而，一种依赖于位点特异性自由基迁移的新方法对结构非常敏感，可以检测手性的变化。进行这项研究的潜在动机是调查白内障疾病的潜在原因，并了解蛋白质修饰如何影响一般的衰老。手性的改变在以前主要是在眼晶状体蛋白的一般意义上进行了检查，并且这些变化已被注意到在白内障晶状体中增加。由于没有合适的工具来执行这项任务，以前没有进行过特定部位手性变化的检查。这个项目的结果将是详细的信息，阐明手性反转如何