同步荧光法研究溴氰菊酯与牛血清白蛋白的结合作用  

Study on the Interaction Between Deltamethrin and Bovine Serumim Albumim by Synchronous Fluorescence Spectroscopy

作　　者：鹿泽启[1] 王雪荣[2] 贾风燕[2] 殷军港[2] 刘永明[2] 

机构地区：[1]山东省烟台市农业科学研究院 [2]烟台大学化学生物理工学院,山东省烟台市清泉路32号264005

出　　处：《光谱实验室》2011年第1期295-298,共4页Chinese Journal of Spectroscopy Laboratory

基　　金：山东省科技攻关项目(NO.2009GG10009053)

摘　　要：用同步荧光法消除了溴氰菊酯对牛血清白蛋白内源性荧光的干扰,研究了生理条件(pH=7.4)下溴氰菊酯与牛血清白蛋白之间的相互作用。不同温度下的猝灭常数证明溴氰菊酯对牛血清白蛋白的猝灭是静态过程,据此求得25℃下溴氰菊酯与牛血清白蛋白的结合常数为1.97×105L.mol-1,热力学参数ΔH=29.79kJ.mol-1、ΔS=201.32J.K-1.mol-1,两者之间的相互作用力以疏水作用力为主。根据Foerster非辐射能量转移机理,计算了牛血清白蛋白与溴氰菊酯间结合距离r=5.42nm,能量转移效率E=0.104。The synchronous fluorescence spectrometry was used to eliminate the interference between the emission of the deltamethrin（DM） and the determination of the endogenous fluorescence of the protein,and study the interaction between deltamethrin and bovine serum albumim in physiological condition（pH 7.4）.The quenching constant at different temperatures proved that the quenching mechanism of fluorescence of BSA by deltamethrin was a static quenching procedure.The association constant（KB）,the enthalpy change and the entropy change at 25℃ were calculated to be KB=1.97×105L.mol-1,ΔH=29.79kJ.mol-1,ΔS=201.32J.K-1.mol-1,which showed that the binding mode was mainly the reflection of the hydrophobic interaction.According to the Foerster＇s non-radiative energy transfer mechanism,the binding distance（r） and the rate of energy transfer（E） between BSA and DM were obtained to be r=5.42nm,E=0.104,respectively.

关 键 词：溴氰菊酯 牛血清白蛋白 同步荧光 荧光猝灭 

分 类 号：O657.32[理学—分析化学]