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.

这项研究的目的是调查白内障 使用拉曼光谱法形成和衰老。 它是 已提出导致二硫化物的透镜结晶蛋白的氧化 交叉连接和蛋白质构象的相关变化是 Moajor在镜头上衰老的Anf白内障形成。 我们已经获得了 单体形式和二聚体的本地伽马II结晶蛋白的拉曼光谱 由HPLC确定的形式和控制样品。 拉曼光谱法 在511 cm-1处检测到二硫化物形成（S-S）。 我们跟随 通过遵循S-S的外观来氧化结晶蛋白 511 cm-1的频率和消失的S-H频率在2500-2600附近 CM-1。 最初的拉曼结果还表明二硫化物 形成或氧化不会导致重大变化 蛋白质的继发构象。 目前我们正在尝试 确定二硫化物交叉链接是分子内还是 分子间并估计该比率是由于这两者都引起的。