光谱法研究一种含咪唑啉酮类衍生物与牛血清白蛋白的相互作用  

Study on the interaction between a kind of imidazolin-ones derivatives and bovine serum albumin by spectroscopic methods

作　　者：孙绍发[1] 於敏敢[1] 朱先军[2] 

机构地区：[1]咸宁学院化学与生命科学系,湖北咸宁437005 [2]华中师范大学化学学院,武汉430079

出　　处：《华中师范大学学报（自然科学版）》2007年第3期406-410,共5页Journal of Central China Normal University：Natural Sciences

基　　金：湖北省自然科学基金项目(2006ABA333);湖北省教育厅重点项目(D200528003);咸宁学院重点科研项目(KL0416).

摘　　要：应用荧光光谱及紫外可见光谱的方法研究了2-氨基-5-苯亚甲基-4H-咪唑啉-4-酮衍生物(BPH5)与牛血清白蛋白(BSA)的相互作用.实验发现BPH5能强烈猝灭牛血清白蛋白的荧光强度,其荧光猝灭机理为动态猝灭.在此基础上计算了二者相互作用的结合常数、结合位点数及ΔH,ΔG,ΔS等热力学参数等.结果表明BPH5与BSA以1∶1结合,其反应主要是熵驱动的,相互作用力主要为疏水作用力.根据F rster无辐射能量转移理论计算了给体(BSA)与受体(BPH5)之间的结合距离.The interaction between （Z）-4-benzylidene-1-（4-chlorophenyl）-2-propylamino- 1H-imidazol-5（4H）-one（BPHS） and bovine serum albumin （BSA） was studied by florescence spectroscopy and UV-vis absorption spectroscopy. The fluorescence intension of BSA could be quenched strongly by BPH5 in the experiment and the mechanism is a dynamic quenching procedure. The values Of binding sites n and apparent binding constant KB were measured by fluorescence quenching method. The thermodynamics parameter AH, AG, AS were calculated. The results indicated BPH5 and BSA were combined by 1 ： 1, the reaction was driven by entropy and the interaction force was mostly hydrophobic force. The distance r between donor （BSA） and acceptor（BPH5） was obtained according to Forster theory of non-radiation energy transfer.

关 键 词：荧光猝灭 热力学参数 牛血清白蛋白 咪唑啉酮衍生物(BPH5) 

分 类 号：O657.39[理学—分析化学]