Identification of peptide epimers in crystallin proteins

晶状体蛋白中肽差向异构体的鉴定

基本信息

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
项目类别：
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&apos 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

项目摘要

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对肽和蛋白质中各个氨基酸手性的修改。手性或分子的惯用性是影响结构和功能的关键属性。手性变化很难检测到。但是，一种取决于特定自由基迁移的新方法对结构非常敏感，并且可以检测手性的变化。进行这项研究的基本动机是研究白内障疾病的潜在原因，并了解蛋白质修饰如何影响衰老。先前主要是在眼镜蛋白的通用意义上检查了手性的变化，并且已经注意到这些变化可以增加白内障晶状体。以前没有对手性变化进行特定于现场的检查，因为没有适当的工具可用于执行任务。该项目的结果将是详细的信息，阐明了手性反转的方式总体上有助于白内障形成和衰老，这对于指导潜在的预防治疗的发展是必不可少的。