光谱和伏安法研究沙丁胺醇与牛血清白蛋白的相互作用

Spectroscopic and voltammetric analysis of the interaction between salbutemol and bovine serum albumin

模拟人体生理条件(pH=7.4)下,用伏安法、荧光、紫外和圆二色谱法研究沙丁胺醇(SAL)与牛血清白蛋白(BSA)的相互作用。用Stern-Volmer和双对数方程处理荧光数据,得到沙丁胺醇与BSA的结合常数为3.12×106L·mol-1、结合位点数约为1。循伏安法确定了SAL与BSA的结合比,并计算了结合常数,结果与用双对数方程计算得到的常数吻合。用紫外和圆二色谱验证了BSA与沙丁胺醇作用时构象的改变。

Under the imitated physiological conditions（ pH = 7. 4）,the interaction between salbutemol（ SAL） and bovine serum albumin（ BSA） was investigated by the fluorescence,UV-vis spectroscopy,voltammetry and circular dichroism. Voltammetric results indicated the formation of the SAL2-BSA complex. Experimental data were processed with Stern-volmer plot and Line weaver-Burk equation. The way of fluorescence quenching was static quenching,and then calculated the binding constant（ 3. 12 10^6L·mol^-1） and binding sites（ -1） and the thermodynamics parameters. The changes in the secondary structure of BSA after its binding with the ligand were studies with UV-vis and circular dichroism spectroscopy. The secondary structure alteration of BSA in the presence of salbutemol were observed.