RAMAN SPECTROSCOPIC INVESTIGATION OF LENS AGING & CATARACT FORMATION

镜片老化的拉曼光谱研究

• 批准号: 6281796
• 负责人: Jayanti Pande
• 金额: $ 0.38万
• 依托单位: MASSACHUSETTS INSTITUTE OF TECHNOLOGY
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-06-01 至 1999-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6281796
• 关键词: aging; bioengineering /biomedical engineering; biological products; biomedical resource

The objective of this research is to investigate the cataract formation and aging of eye lens using Raman spectroscopy. It is has been proposed that oxidation of lens crystallins leading to disulfide cross linking and associated changes in protein conformation are moajor steps in lens aging anf cataract formation. We have obtained Raman spectra of native gamma II crystallin in monomer form and dimer form determined by HPLC, and control samples. Raman spectroscopy detected disulfide formation (S-S) at 511 cm-1. We followed the oxidation of crystallin protein by following the appearance of S-S frequency at 511 cm-1 and disappearance S-H frequency near 2500-2600 cm-1. The initial Raman results also suggested that disulfide formation or oxidation does not result in significant changes in secondary conformation of the protein. Currently we are trying determine whether the di-sulfide cross linking is intramolecular or inter molecular and estimate the ratio if it is due to both.

本研究的目的是探讨白内障 使用拉曼光谱学研究眼睛透镜的形成和老化。 它有 已经提出透镜晶体蛋白的氧化导致二硫化物 交联和蛋白质构象的相关变化是 主要参与透镜老化和白内障形成。 我们所获得 天然γ II晶体蛋白单体和二聚体的拉曼光谱 通过HPLC测定的形式和对照样品。 拉曼光谱 在511 cm-1处检测到二硫化物形成（S-S）。 我们跟着 晶状体蛋白的氧化，遵循S-S的出现 在511 cm-1处的频率和在2500-2600附近的S-H消失频率 cm-1. 最初的拉曼结果还表明， 形成或氧化不会导致 蛋白质的二级构象。 目前，我们正在努力 确定二硫化物交联是分子内的还是 如果是由于两者，则估计比率。