Identification of peptide epimers in crystallin proteins

描述(申请人提供)：该项目的总体目标是使用一种创新的质谱学技术来检测和表征多肽和蛋白质中个别氨基酸的手性修饰。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到；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衰老。手性的变化以前主要是在眼晶状体蛋白质的一般意义上进行检查的，这些变化在白内障晶状体中增加了。以前没有对手性变化进行特定部位的检查，因为没有合适的工具来执行这项任务。这个项目的结果将是详细的信息，阐明手性反转如何 有助于白内障的形成和普遍衰老，这对于指导潜在的预防性治疗的发展是必要的。

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.