荧光光谱法分析盐酸哌唑嗪与牛血清白蛋白的结合作用  

Interaction of Prazosin Hydrochloride with Bovine Serum Albumin by Fluorescence Spectroscopy

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

机构地区：[1]河北石家庄白求恩军医学院训练部,石家庄050081 [2]河北医科大学药学院,石家庄050017

出　　处：《中国现代应用药学》2007年第6期438-442,共5页Chinese Journal of Modern Applied Pharmacy

摘　　要：目的研究不同温度下盐酸哌唑嗪与牛血清白蛋白(BSA)间的相互作用及其作用机制。方法荧光光谱法。结果荧光光谱法测定盐酸哌唑嗪与BSA在25℃和37℃反应的结合常数K均是2.0×104L.mol-1,结合位点数n分别为1.19,1.14,热力学参数为(37℃)ΔH=0,ΔG=-25.52kJ.mol-1,ΔS=0.082kJ.mol-1.K-1,盐酸哌唑嗪的加入影响了BSA的构象;依据Frster非辐射能量转移机制,得到盐酸哌唑嗪与BSA之间的结合距离和能量转移效率分别为r=4.69nm,E=0.078。结论盐酸哌唑嗪与BSA在实验浓度范围内形成了具有一定结构的复合物,且它们之间的作用力以静电作用力为主。OBJECTIVE To study the mechanism of interaction between prazosin hydrochloride and bovine serum albumin （BSA） at different temperatures by Fluorescence spectroscopy. METHODS Fluorescence spectroscopy was used. RESULTS The binding constant is 2.0 × 10^4L · mol^-1, the numbers of binding sites at 25% and 37% were 1, 19 and 1.14 respectively. At 37℃ ,the thermodynamic parameters of interaction between prazosin hydrochloride and BSA were △H = 0,△G = - 25.52 k,J · mol^ -1 ,△S = 0. 082 k,J ·mol^ -1 · K^-1. The effect of prazosin hydrochloride on the conformation of BSA was analyzed. According to the theory of Fdrester nonradiation energy transfer,the binding distance and transfer efficiency between prazosin hydrochloride and BSA were r = 4.69 nm and E = 0. 078 respectively. CONCLUSION BSA could react with prazosin hydrochloride to form a complex in the range of experimental concentrations ,the quenching mechanism of them were suggested as static quenching, its action force was mainly electro-static interaction.

关 键 词：盐酸哌唑嗪 牛血清白蛋白 荧光 

分 类 号：R972.4[医药卫生—药品] R917.1[医药卫生—药学]