灯盏花素与牛血清白蛋白相互作用的荧光光谱研究

摘要

采用荧光光谱法和紫外吸收光谱法研究了灯盏花素(BR)与牛血清白蛋白(BSA)的相互作用；利用热力学方程计算了295 K和308 K下的热力学参数△H、△G和△S,根据Stern-Volmer方程求出了猝灭常数和结合常数.结果表明,BR对BSA的荧光具有猝灭作用,其猝灭机制为动态-静态联合猝灭,BSA发射峰略有蓝移. BR与BSA之间的作用力主要为疏水作用.%The interaction between breviscapine (BR) and bovine serum albumin (BSA) was investigated by means of fluorescence spectrometry and ultraviolet absorption spectrometry. The thermodynamic parameters AH, AG and AS at 295 K and 308 K were calculated using thermo-dynamic equations. The quenching constant, binding constant and binding sites were obtained according to Stern-Volmer equation. Results indicate that the fluorescence of BSA is quenched by BR, and BR functions to quench the fluorescence of BSA by a static-and-dynamic joint quenching process, with the maximum emission wavelength of BSA being slightly blue-shifted. Besides, the interaction between BR and BSA is dominated by hydrophobic force.