血清白蛋白与巴比妥钠相互作用的光谱研究  

Spectrophotometric Studies on the Interaction of Barbital Sodium and Bovine Serum Albumin

作　　者：迟燕华[1] 庄稼[2] 丁飞[1] 

机构地区：[1]西南科技大学化学系,四川绵阳621010 [2]西南石油大学材料科学与工程学院,四川成都610500

出　　处：《分析测试学报》2007年第5期658-661,共4页Journal of Instrumental Analysis

基　　金：电分析化学国家重点实验室基金项目(2005007);四川省科学技术重点攻关项目(03GG009-024);教育部科学技术研究重点资助项目(02126)

摘　　要：采用荧光光谱、紫外-可见光谱研究了药物巴比妥钠(BBTS)和牛血清白蛋白(BSA)的相互作用机理,运用热力学方法确定了巴比妥钠和牛血清白蛋白相互作用力的类型主要是疏水力,该过程是一个熵增加、Gibbs自由能降低的自发超分子作用过程,根据Stern-Volmer方程和Lineweaver-Burk双倒数曲线方程求出了其结合常数在高温时比在低温时小,用F ster非辐射能量转移理论计算了二者结合时给体和受体之间的距离r=2.76 nm,能量转移效率E=0.332,证实了巴比妥钠和牛血清白蛋白之间的作用是生成复合物的静态猝灭过程,说明了猝灭机制是通过能量转移产生的。The mechanism of the interaction of barbital sodium（BBTS） and bovine serum albumin（BSA） was studied by fluorescence and UV-Vis absorption spectroscopy,respectively.By using the thermodynamics parameters,the main type of the interaction force was confirmed to be a hydrophobic one.The process of binding BBTS to BSA was a spontaneous supermolecular interaction with an increase of entropy and a decrease of Gibbs free energy.According to the Stern-Volmer equation and the Lineweaver-Burk double-reciprocal equation,the binding constant at high temperature was smaller than that at low temperature.The binding distance（r=2.76 nm） and the energy transfer efficiency（E=0.332） were calculated by the Frster non-radiative energy transfer theory.It was confirmed that the interaction of BBTS and BSA was a static quenching process based on the energy transfer.

关 键 词：巴比妥钠 牛血清白蛋白 荧光光谱 紫外-可见光谱 热力学参数 

分 类 号：O657.3[理学—分析化学]