芬布芬-铜(Ⅱ)-牛血清白蛋白相互作用的光谱法研究  

Spectroscopic method Studies on the interaction Between Ternary Complex of FBF,Copper(Ⅱ)and Bovine Serum Albumin

作　　者：王晓霞[1] 王正德[1] 刘云颖[1] 

机构地区：[1]内蒙古科技大学化学与化工学院,内蒙古包头市阿尔丁大街7号014010

出　　处：《光谱实验室》2013年第6期3330-3334,共5页Chinese Journal of Spectroscopy Laboratory

基　　金：教育部"春晖计划"基金资助项目(No.2009-1-01040);内蒙古教育厅高校科研基金项目(No.NJZY11145);内蒙古科技大学创新基金资助项目(No.2012NCL034)

摘　　要：模拟生理条件下,应用荧光光谱法研究了芬布芬对牛血清白蛋白,铜(Ⅱ)对牛血清白蛋白以及铜(Ⅱ)对芬布芬和牛血清白蛋白荧光光谱特性的影响。实验表明:铜(Ⅱ)和芬布芬均可使牛血清白蛋白的荧光强度发生静态猝灭,并且在铜(Ⅱ)存在下,芬布芬对牛血清白蛋白的荧光猝灭作用显著增强。根据荧光猝灭双倒数图计算芬布芬和牛血清白蛋白的结合常数为8.44×104,结合位点数为0.97。荧光猝灭双倒数图计算的结果表明,芬布芬和牛血清白蛋白之间的结合常数和结合位点数均随铜(Ⅱ)浓度的增大而增大。很据三者结合反应的研究,进一步探讨了芬布芬、铜(Ⅱ)在生物体内与蛋白质相互作用的机理。The influences of fenbufen （FBF） on the fluorescence of bovine serum albumin （BSA） ,copper（ Ⅱ ）on that of bovine serum albumin,and copper （ Ⅱ ）on the of fenbufen and bovine serum albumin were studied under imitated the physiological condition. It was shown that both fenbufen and copper （ Ⅱ ）have a powerful ability to quench the BSA fluorescence via a nonradiative energy transfer mechanism. But the fluorescence quenching action of fenbufen on BSA was much stronger in the presence of copper （ Ⅱ ）. The fluorescence quenching data were analyzed according to double-reciprocal equation,and the binding constant （K） and the binding sites（n）were obtained. In the system of binary complex of FBF and BSA K= 8.44 × 10^4 and n=0.97,According to Stern-Volmer equation and double-reciprocal equation,the concentration of copper （ Ⅱ ） is denser, and the binding constant （K） and the binding sites （n） are bigger. By studying the binding interaction between copper （ Ⅱ ）,fenbufen and BSA,the mechanism of the interaction among fenbufen,eopper（ Ⅱ ）and protein in organism ,is furtherly discussed.

关 键 词：荧光光谱法 芬布芬 铜(Ⅱ) 牛血清白蛋白 二元配合物 三元配合物 

分 类 号：O657.32[理学—分析化学]