【摘要】 利用亲和毛细管电泳法(ACE)研究了柳叶水甘草碱(TAB)与牛血清白蛋白(BSA)的相互作用。结果表明,柳叶水甘草碱与BSA常温下结合常数为8.00×106L·mol-1,热力学参数验证两者相互作用力以氢键和范德华力为主。傅立叶变换红外光谱(FT-IR)进一步考察了柳叶水甘草碱对BSA二级结构的影响,其结果是,柳叶水甘草碱使得蛋白的α-螺旋、β-转角含量降低,β-折叠含量上升。在分子水平,利用分子对接技术确定了柳叶水甘草碱和牛血清白蛋白结合的适宜位置。更多还原

【Abstract】 Affinity capillary electrophoresis was employed to study the interaction between tabersonine(TAB) and bovine serum albumin(BSA).The results showed that the binding constant is 8.00×106 L·mol-1 under normal temperature.The thermodynamic parameters indicated that the interaction between tabersonine and BSA was driven mainly by hydrophobic interaction and van der Waals forces.The secondary structure of BSA was changed in the presence of TAB according to the FT-IR results.It was shown that TAB reduced α-helix,β-turn and increased β-sheet.At the molecular level,the binding mode of TAB and BSA was determined by molecular modeling method.更多还原