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.