克百威与牛血清白蛋白相互作用的光谱学研究

摘要

[ Objective ] The research aimed to discuss the interaction between bovine serum albumin (BSA) and carbofuran. [ Method ] Using synchronous fluorescence spectrometry,the interaction between carbofuran and BSA in Tris - HC1 buffer system (pH 7.40)was investigated. The binding constants at different temperatures were calculated and the interaction types between carbofuran and BSA were discussed. [ Result ] Under simulative physiological conditions, stronger quenching effect of carbofuran on BSA was electrostatic interaction. According to the changes of different drug concentrations and temperature,it was concluded the quenching way was static quenching. The binding constants (Ksv) at 25,37 and 50 ℃ were 1.17 × 104 、1.07 × 10 and 0.99 × 104 L/mol respectively. Carbofuran was bound with BSA by the ratio of 1: 1. [Conclusion] The research had certain guiding significance for understanding the transport and metabolism of carbofuran in vivo at the molecular level.%[目的]探讨克百威与牛血清白蛋白的相互作用.[方法]采用同步荧光光谱法,研究在pH 7.40 Tris - HC1缓冲体系下克百威与牛血清白蛋白的相互作用,计算不同温度下的结合常数,并探讨了克百威与BSA之间的作用力类型.[结果]在正常生理条件下克百威对牛血清白蛋白的较强的猝灭作用为静电作用.根据不同的药物浓度及温度的变化,判断其猝灭方式可能为静态猝灭.在25、37、50℃温度下反应的结合常数KSV分别为1.17 × 104、1.07×104和0.99×104 L/mol,克百威与BSA按1:1的比例结合.[结论]该研究对从分子水平上了解克百威的体内转运与代谢具有一定的指导意义.