Institute of Nuclear Physics Polish Academy of Sciences, PL-31342 Krakow, Poland.
Institute of Nuclear Physics Polish Academy of Sciences, PL-31342 Krakow, Poland.
Spectrochim Acta A Mol Biomol Spectrosc. 2018 Jan 5;188:332-337. doi: 10.1016/j.saa.2017.07.027. Epub 2017 Jul 19.
In this study we present vibrational analysis of healthy (non-affected by cataract) and cataractous human lenses by means of Raman and FTIR spectroscopy methods. The performed analysis provides complex information about the secondary structure of the proteins and conformational changes of the amino acid residues due to the formation of opacification of human lens. Briefly, the changes in the conformation of the Tyr and Trp residues and the protein secondary structure between the healthy and cataractous samples, were recognized. Moreover, the observed spectral pattern suggests that the process of cataract development does not occur uniformly over the entire volume of the lens.
在这项研究中,我们通过拉曼和傅里叶变换红外光谱法对健康(未受白内障影响)和白内障人眼晶状体进行了振动分析。所进行的分析提供了有关蛋白质二级结构和由于人眼晶状体混浊形成而导致的氨基酸残基构象变化的复杂信息。简而言之,识别了健康和白内障样品之间 Tyr 和 Trp 残基和蛋白质二级结构的构象变化。此外,观察到的光谱模式表明白内障发展过程并非在整个晶状体体积上均匀发生。