阿维菌素与牛血清白蛋白作用的光谱研究

依据阿维菌素与牛血清白蛋白的结合作用使牛血清白蛋白内源荧光发生改变的现象,用荧光光度法研究了在一定条件下阿维菌素和牛血清白蛋白相互作用的机理。结果表明,阿维菌素对牛血清白蛋白的荧光猝灭是形成了超分子化合物的静态猝灭过程。测定了在不同温度下阿维菌素与牛血清白蛋白的结合常数KA和结合位点数n分别为KA=2.26×103L·mol-1,n=1.08(25℃);KA=1.35×103L·mol-1,n=1.05(35℃)。根据阿维菌素与牛血清白蛋白相互作用的热力学参数,确定了阿维菌素与牛血清白蛋白之间的作用力类型为氢键和范德华力;根据Foerster非辐射能量转移理论求得阿维菌素与牛血清白蛋白的结合距离为2.55nm。用同步荧光光谱确定阿维菌素影响了BSA微区的构象。

Spectral Study on Interaction Between Abamectin and Bovine Serum Albumin

The interaction between abamectin and bovine serum albumin（BSA） was studied base on the phenomenon of the fluorescence changes of BSA by fluorescence spectrometry.The fluorescence quenching mechanism of abamectin with BSA is a static quenching procedure,and the apparent binding constants （KA） between abamectin and BSA are 2.26×103L·mol-1（25℃） and 1.35×103L/mol（35℃）,and the binding sites （n） are 1.08（25℃） and 1.05（35℃）.According to thermodynamic parameters,the interaction force between abamectin and BSA was mainly the hydrogen bond and Van der Waals force,and the distance between them was 2.55nm by Foerster non-radiative energy transfer theory.The influence of abamectin on micro-area of BSA was also studied by the synchronous fluorescence spectrum.