光谱法研究核壳量子点CdTe/CdS与牛血清白蛋白的相互作用  

Study on the Interaction of Bovine Serum Albumin with Core-shell CdTe/CdS QDs by Spectroscopic Methods

作　　者：田建袅[1] 周柳金[1] 廉营 赵彦春[1] 赵书林[1] 

机构地区：[1]药用资源化学与药物分子工程教育部重点实验室广西师范大学化学化工学院

出　　处：《化学通报》2012年第3期262-267,共6页Chemistry

基　　金：国家自然科学基金项目(21165004);广西自然科学基金创新团队项目(2010GXNSFF013001);广西自然科学基金项目(0728043);广西教育厅科研项目(桂教科研[2006]26号)资助

摘　　要：应用荧光光谱、圆二色光谱和紫外吸收光谱等技术研究核壳量子点CdTe/CdS与牛血清白蛋白(BSA)相互作用的结果表明,CdTe/CdS对BSA的荧光猝灭机理为静态猝灭。根据不同温度下量子点对BSA的荧光猝灭作用计算了结合常数、热力学参数,证明了量子点与BSA相互作用力主要是范德华力或氢键作用力。探讨了量子点对BSA构象的影响。The interaction of bovine serum albumin（BSA） and Core-shell CdTe/CdS quantum dots（QDs） was investigated by absorption,circular dichroism（CD） and fluorescence spectroscopy.The static quenching exists between QDs and BSA in physiological solution.The quenching constant was obtained at different temperatures（298,305,310 K）.According to the thermodynamic parameters,it showed that binding power between QDs and BSA is mainly by Van der Waals force or hydrogen bonds forces.The results showed that QDs can quench the fluorescence of BSA with a static quenching mechanism.Synchronous fluorescence spectra,ultraviolet absorption spectroscopy and circular dichroism were used to investigate the conformational changes of BSA.

关 键 词：量子点 牛血清白蛋白 荧光光谱法 紫外-可见光谱法 圆二色光谱 

分 类 号：Q503[生物学—生物化学]