金属离子对齐多夫定与牛血清白蛋白结合作用的影响  

Effecting of Metal Ions on the Interaction between Zidovudine and Bovine Serum Albumin

作　　者：邵爽[1] 邱瑾[2] 

机构地区：[1]浙江教育学院化学系,杭州310012 [2]杭州师范大学化学系,杭州310036

出　　处：《物理化学学报》2009年第7期1342-1346,共5页Acta Physico-Chimica Sinica

基　　金：浙江省自然科学基金(M203145)资助项目~~

摘　　要：用荧光光谱法和紫外分光光度法研究了水溶液(Tris-HCl缓冲溶液,pH7.1)中齐多夫定(ZDV)与牛血清白蛋白(BSA)的结合作用及三种金属离子(Cu2+,Mg2+,Zn2+)对其的影响.结果表明:齐多夫定及金属离子均导致BSA的内源荧光猝灭,猝灭机制均为静态猝灭;齐多夫定与BSA间存在较强结合作用,热力学参数ΔH和ΔS分别为-10.2kJ·mol-1和77.5J·mol-1·K-1(298K),表明其结合力以静电作用力为主;298K下结合常数、结合位点数和结合距离分别为6.92×105L·mol-1、1.18和2.28nm;温度升高结合常数和结合位点数减小.三种金属离子均导致ZDV与BSA的结合常数减小,结合距离增大.The interaction between zidovudine （ZDV） and bovine serum albumin （BSA） was investigated by fluorescence spectroscopy and ultraviolet-visible spectroscopy in aqueous solution （Tris-HC1 buffer, pH 7.1）. The effect of metal ions （Cu2＋, Mg2＋, Zn2＋） on the interaction was also investigated. Results showed that the fluorescence intensity of BSA at 346 nm was quenched when zidovudine or metal ions were added. The quenching mechanism was a static quenching mechanism. A strong interaction exists between zidovudine and BSA. The thermodynamic parameters AH and AS were -10.2 kJ·mol^-1 and 77.5 J·mol-1·K-1 at 298 K, respectively, indicating that electro-static forces played a major role. The binding constant, the number of binding site and the binding distance were 6.92×10^5 L·mol-1, 1.18, and 2.28 nm at 298 K, respectively. The binding constant and the number of binding sites decreased with the increase in temperature. The metal ions, Cu^2＋, Mg2＋ and Zn2＋, all decreased the binding constant and increased the binding distance for binding between ZDV and BSA.

关 键 词：牛血清白蛋白 齐多夫定 金属离子 荧光猝灭 

分 类 号：R96[医药卫生—药理学]