结晶紫与牛血清蛋白相互作用研究

Inter action between Crystal Violet and Bovine Serum Albumin

运用荧光光谱和紫外-可见吸收光谱研究了在缓冲溶液中不同温度下结晶紫(CV)与牛血清白蛋白(BSA)之间的相互作用。实验结果表明,CV对BSA的内源荧光猝灭为静态猝灭过程。测定了该反应在不同温度下的结合常数KA,KA分别为1.49×105L.mol-1(25℃)、1.15×105L.mol-1(35℃)和1.01×105L.mol-1(45℃),CV与BSA以摩尔比1∶1结合。根据Forster非辐射能量转移理论,求出了37℃时给体(CV)和受体(BSA)之间结合距离为r=6.48nm。计算出的热力学参数表明,CV和BSA之间的作用力主要是通过疏水作用力相互作用。

The interaction between Crystal Violet （CV） and bovine serum albumin （BSA） was investigated via fluorescence and ultraviolet-visible absorption spectra in buffer solutions at different temperatures. The experimental results showed that static quenching was involved in adding CV in BSA solution. The binding constants KA, the num- ber of binding sites n,and corresponding thermodynamic parameters AGe, AHe, ASebetween CV and BSA at differ- ent temperatures were calculated. The binding constants （ KA ） were 1.49×105L.mol-1（25℃）、1.15×105L.mol-1（35℃） and 1.01×105L.mol-1（45℃）, respectively, and they reacted at amolar ratio of 1 ： 1. The binding distance r was 6. 48nm between CV and BSA according to Forster non-radiative energy transfer mechanism. The inter- action between CV and BSA was driven mainly by hydrophobic interaction according to thermodynamic parameters.