光谱法研究喜树碱与牛血清白蛋白的相互作用  

Spectroscopic investigation of the interaction between camptothecin and bovine serum albumin

作　　者：于岚岚[1] 杨冉[1] 陈晓英[1] 李建军[1] 屈凌波[1,2] 

机构地区：[1]郑州大学化学系,郑州450001 [2]河南工业大学化学化工学院,郑州450052

出　　处：《分析试验室》2012年第1期42-46,共5页Chinese Journal of Analysis Laboratory

基　　金：国家自然科学基金(批准号:21002093);教育部留学回国人员科研启动基金;中国博士后科学基金项目资助

摘　　要：采用多种光谱技术对喜树碱和牛血清白蛋白的相互作用进行了研究。结果表明喜树碱和牛血清白蛋白可形成基态复合物,引起牛血清白蛋白内源荧光猝灭。通过计算获得了二者在不同温度下的结合常数及结合位点数。根据喜树碱和牛血清白蛋白结合的热力学参数,确定了二者之间主要为疏水作用力。根据Frster非辐射能量转移理论确定了喜树碱和牛血清白蛋白的作用距离。同步荧光光谱显示喜树碱主要与蛋白中色氨酸残基发生相互作用,改变其周围的局部构象。红外光谱提示喜树碱可引起蛋白的构象发生改变,α-螺旋二级结构减少。The interaction between camptothecin and bovine serum albumin was investigated by several spectroscopic techniques.The results showed that camptothecin formed ground-state complex with bovine serum albumin to induce the quenching of the intrinsic fluorescence of the protein.The binding constants and the numbers of binding site at different temperatures were calculated.According to the thermodynamic parameters,hydrophobic interaction was determined as the main binding force.The distance between camptothecin and bovine serum albumin was determined based on Frster non-radiation energy transfer theory.The results from synchronous fluorescence spectra indicated that camptothecin mainly interacted with tryptophan in bovine serum albumin,leading to a local change in protein conformation.The infrared spectra also demonstrated that camptothecin induced a conformational change for bovine serum albumin with a decrease of α-helix structure.

关 键 词：喜树碱 荧光光谱法 同步荧光光谱法 药物-蛋白相互作用 

分 类 号：O657.3[理学—分析化学]