【摘要】 应用荧光光谱法研究了十六烷基三甲基溴化铵(CTAB)与牛血清白蛋白(BSA)的相互作用机制。实验结果表明,CTAB主要以静态猝灭的方式使得BSA的荧光强度显著降低;求得它们在l6℃和25℃温度下的结合常数以及结合位点数n;计算得出CTAB与牛血清白蛋白的相关热力学参数(25℃);CTAB和BSA主要凭借范德华力和氢键作用结合。同时以芘为荧光探针、二苯甲酮为猝灭剂,用稳态荧光探针法测定了CTAB的临界胶团浓度(CMC)与不同表面活性剂浓度下的胶团聚集数(N)并研究了BSA对其临界胶团聚集数的影响。且用同步荧光技术考察了十六烷基三甲基溴化铵对牛血清白蛋白构象的影响。更多还原

【Abstract】 The mechanism of the interaction between cetyltrimethylammonium bromide (CTAB) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy.The result of this experiment showed that:the binding constants and the numbers of binding sites were accounted,respectively,at l6℃ and 25℃ by intrinsic fluorescence method.The thermodynamic parameters of interaction between CTAB and BSA were calculated (25℃).The effect of CTAB on the conformation of BSA was also analyzed by synchronous fluorescence spectrometry.The analysis of fluorescence data indicated the presence of static quenching mechanism in the binding and the main dominant sorts of binding forces were hydrogen bond and Van der Waals’interaction.At the same time,the critical micelle concentration (CMC),micelle aggregation numbers (N) at different surfactant concentrations were also determined by pyrene probe fluorescence method and benzophenone was used as the quencher here.更多还原