中文摘要：

采用分子对接方法研究了药物小分子七叶苷与牛血清白蛋白（BSA）之间的相互作用,获得了七叶苷与BSA的结合模式信息.分子对接结果表明,七叶苷分子与蛋白活性空腔内的氨基酸残基形成疏水作用和氢键作用.这些基团之间的相互作用是七叶苷与BSA稳定结合的关键因素.研究结果可为相关实验研究提供微观结构信息.

英文摘要：

Molecular docking was used to investigate the interaction of esculin with bovine serum albumin（BSA）.The results indicate that esculin can produce hydrophobic interactions with the nonpolar side chains of the residues（such as Leu 197,Trp 213,Ala 209 and Leu 480）in the binding pocket.Moreover,several residues（Glu 449,Val 481,Arg 483,Ser 201,Ser 453 and Ser 343）around esculin can form H-bonds with esculin,which can produce significant contribution to biological activities.The hydrophobic and H-bonds interactions between ligand and protein are the key to make the complex stable.These results will provide theoretical basis for the further experimental researches.