荧光光谱法研究阿莫西林与牛血清白蛋白的相互作用  

The Interaction of Amoxicillin and BSA by Fluorescence Spectrometry

作　　者：刘建波[1] 张君才[1] 王晓玲[1] 张萍[1] 

机构地区：[1]咸阳师范学院化学与化工学院,陕西省咸阳市文林路东段712000

出　　处：《光谱实验室》2013年第3期1157-1160,共4页Chinese Journal of Spectroscopy Laboratory

基　　金：陕西省教育厅科研基金项目(11JK0580);咸阳师范学院专项基金(10XSYK306)

摘　　要：本文采用分子荧光光谱法对阿莫西林与牛血清白蛋白(BSA)之间的相互作用进行了研究,得知阿莫西林对BSA有猝灭作用,其猝灭方式为静态猝灭,并求出了猝灭常数,结合常数及结合位点数。通过298K和310K时的实验数据求出热力学参数ΔH、ΔG和ΔS,结果表明阿莫西林主要通过氢键和范德华力与BSA之间结合。The interaction between amoxieillin and bovine serum albumin （BSA） was investigated by fluorescence spectrometry. The fluorescence of BSA was quenched by amoxicillin, which was a static quenching process. The quenching constant, binding constant, binding sites and thermodynamic parameters were obtained according to Stern--Volmer equation. The results showed that the interaction between amoxieillin and BSA was hydrogen bond and Van der Waals force.

关 键 词：阿莫西林 牛血清白蛋白 荧光光谱 

分 类 号：O657.32[理学—分析化学]