氢氯噻嗪与牛血清白蛋白的相互作用  

Study of the Interaction between BSA and Hydrochlorothiazide

作　　者：侯玉娟[1] 朴红光[1] 

机构地区：[1]淮海工学院理学院,江苏连云港222005

出　　处：《实验室研究与探索》2012年第3期21-24,共4页Research and Exploration In Laboratory

基　　金：The Korean government(ministry of education;science and technology)Grant(2009-0072927)

摘　　要：用荧光光谱法研究了氢氯噻嗪(Hydrochlorothiazide,HCT)与牛血清白蛋白(BSA)的相互作用。实验结果表明,HCT与BSA作用的猝灭常数随着温度的升高而降低,HCT可以有规律地使BSA内源荧光猝灭,其猝灭机理可认为是HCT与BSA形成复合物的静态猝灭。通过测定和计算不同温度下该结合反应的结合常数和结合位点数,并根据热力学方程求得了结合反应的ΔG、ΔH和ΔS等热力学参数,根据所得结果推断出HCT与BSA间的主要作用力类型是疏水作用力。同时,从分子荧光寿命进一步证明HCT与BSA的荧光猝灭机制为静态猝灭。The quenching mechanism of the fluorescence of bovine serum albumin（BSA） with hydrochlorothiazide was studied by fluorescence method. A decrease in the quenching constant was observed with an increase in temperature. From the fluorescence spectrum and the fluorescence intensity, the results show that the quenching mechanism of hydrochlorothiazide to BSA was static quenching. The binding constants, the number of binding sites and tile thermodynamic parameters of the reaction of hydrochlorothiazide with BSA, such as AG, AH and AS were calculated at different temperatures. So the binding force was mainly hydrophobic. The effect of hydrochlorothiazide on the conformation of BSA was also studied by using fluorescence lifetime. The results indicate that the quenching mechanism of Hydrochlorothiazide to BSA is static quenching.

关 键 词：荧光光谱 氢氯噻嗪 牛血清白蛋白 热力学参数 荧光寿命 

分 类 号：O614.3[理学—无机化学]