摘要
采用荧光光谱法研究了在模拟人体生理环境条件下,pH 7.40的Tris-HCl缓冲体系中,丹酚酸A(Sal A)与牛血清白蛋白(BSA)的相互作用。结果表明,丹酚酸A对牛血清白蛋白有较强的荧光猝灭作用。用Stern-Volmer和Lineweaver-Burk方程处理数据,推断其猝灭机理为丹酚酸A与牛血清白蛋白形成复合物的静态猝灭,并获得了25、30、35℃下丹酚酸A与牛血清白蛋白作用的结合常数分别为1.49×105、1.19×105、8.24×104 L/mol。根据Van't Hoff方程计算得出ΔH=-56.55kJ/mol,根据所得热力学参数推断丹酚酸A与牛血清白蛋白之间的主要作用力为氢键与范德华力。在25℃时,计算获得丹酚酸A与牛血清白蛋白的结合位点数为1.158。
The interaction between salvianolic acid A(Sal A) and bovine serum albumin(BSA) at pH 7.40 was studied by fluorescence spectroscopy.The fluorescence of BSA is quenched obviously by Sal A,the mechanism of fluorescence quench was deemed as static mode.The fluorescence quenching data were analyzed according to Stern-Volmer equation and Lineweaver-Burk equation.The binding constants of Sal A with BSA are obtained at 25,30,35 ℃ were 1.49×105,1.19×105,8.24×104 L/mol.The thermodynamic parameters,enthalpy change(ΔH) was calculated to be-56.55 kJ/mol.The results indicated that Sal A could bind with BSA strongly at molar ratio 1∶1.The hydrophobic interaction force and Van der Waals force play a main role in the binding of Sal A with BSA.
出处
《大连工业大学学报》
CAS
北大核心
2012年第2期95-97,共3页
Journal of Dalian Polytechnic University
