【摘要】 用荧光和紫外光谱法研究Tris-HCl缓冲溶液中拉米夫定与牛血清白蛋白(BSA)作用机制.测定了不同温度下拉米夫定对BSA的荧光猝灭光谱,并对其猝灭机制进行了讨论,认为拉米夫定对BSA的猝灭为静态猝灭;运用位点结合模型,计算得到298K时拉米夫定与BSA结合常数KA为1.79×105L.mol-1和结合位点数n为1.04,说明二者存在一定相互作用,其作用力主要为氢键或范德华力;根据F ster偶极-偶极非辐射能量转移原理,求得拉米夫定在BSA上距色氨酸残基的距离r为2.21nm;最后通过同步荧光光谱发现拉米夫定对BSA构象产生了一定的影响.更多还原

【Abstract】 The interaction mechanism between lamivudine and bovine serum albumin(BSA) in aqueous solution(Tris-HCl buffer,pH 7.1)is studied with ultraviolet-visible and fluorescence spectrum.The binding constant KA is found to be 1.79×105L·mol-1,and the binding sites n to be 1.04 at 298K by fluorescence quenching method.The interaction between lamivudine and BSA is strong and the main binding force is hydrogen bond or Van de Waals force.According to the theory of Fsters dipile-dipile non-radiation energy transfer,the distance measured between lamivudine and tryptophane is 2.21 nm.The effect of lamivudine on the conformation of BSA is analyzed using synchronous fluorescence spectrometry.更多还原