L-半胱氨酸与牛血清白蛋白相互作用的荧光光谱分析

运用荧光猝灭光谱、同步荧光光谱探讨了L-半胱氨酸（L-Cys）与牛血清白蛋白（BSA）的相互作用，并计算了猝灭常数、结合常数、结合位点数以及3个热力学参数△H、△G和△S。结果表明,L-Cys使BSA的内源荧光发生猝灭,BSA的发射峰从350nm蓝移到347．5nm，荧光猝灭机制为动态猝灭；L-Cys与BSA之间的作用力主要为疏水作用力；L-Cys对BSA结构的微环境有一定的影响。

Fluorescence Spectrometric Analysis on the Interaction between L-Cysteine and Bovine Serum Albumin

The interaction between L-cysteine（L-Cys） and bovine serum albumin（BSA） was investigated by fluorescence quenching spectrum and synchronous fluorescence spectrum. The quenching constant, binding constant,binding sites of L-Cys with BSA, and the thermodynamic parameters （△H, △G,△S） were calculated. The fluorescence of BSA was quenched by L-Cys. The fluorescence peak of BSA shifted from 350 nm to 347.5 nm. Its quenching mechanism was a dynamic process. Their interaction force was hydrophobic force. The synchronous fluorescence spectrum showed that L-Cys influenced the mieroenvironment around BSA.