荧光猝灭法研究α_1受体拮抗剂与牛血清白蛋白的相互作用  

Interaction of blocking agents of α_1 acceptor with bovine serum albumin by fluorescence quenching analysis

作　　者：安普丽[1] 张剑[2] 蒋晔[1] 任淑萌[1] 李珺沬[1] 

机构地区：[1]河北医科大学药学院,河北石家庄050017 [2]河北医科大学科技总公司,河北石家庄050017

出　　处：《华西药学杂志》2008年第1期37-40,共4页West China Journal of Pharmaceutical Sciences

摘　　要：目的研究α1受体拮抗剂(盐酸特拉唑嗪、盐酸哌唑嗪、盐酸阿夫唑嗪)与牛血清白蛋白(BSA)的相互作用及机制。方法用荧光猝灭反应和F rster非辐射能量转移机制。结果α1受体拮抗剂与BSA间的猝灭过程是静态猝灭过程;求得25℃时与BSA间的结合常数KA分别为1.8×104、2.0×104、2.5×104L.mol-1;结合位点数n分别为1.29、1.14、1.32;结合距离r分别为4.91、4.69、4.71 nm;能量转移效率分别为0.058、0.078、0.085。结论α1受体拮抗剂与BSA间的主要结合力为静电作用力,与蛋白结合作用机制相似。OBJECTIVE The interaction mechanism between BSA and agents of α1 acceptor （Terazosin hydrochloride, Prazosin hydrochloride and Alfuzosin hydrochloride） were studied by means of fluorescence quenching method. METHODS Fluorescence quenching and the theory of Foerster non - radiation energy transfer were used. RESULTS With fluorescence quenching method, the binding constants （KA） were 1.8 × 10^4, 2. 0 × 10^4 ,2. 5 × 10^4 L·mol^-1 and the binding sites （n） were 1.29, 1.14,1.32 respectively, at 25℃. According to the theory of Foerster non - radiation energy transfer, the binding distances were 4. 91, 4.69, 4.71 nm and the transfer efficiencies were 0. 058, 0. 078, 0. 085 respectively. CONCLUSION The electrostatic interaction is found to be the main acting force in the studied systems. All the results show that the mechanisms of the interaction between agents of α1 acceptor and BSA are similar.

关 键 词：盐酸特拉唑嗪 盐酸阿夫唑嗪 盐酸哌唑嗪 荧光猝灭 牛血清白蛋白 

分 类 号：R917[医药卫生—药物分析学] R96[医药卫生—药学]