大豆皂苷Ⅱ与人血清白蛋白相互作用机制研究  

Interaction between soyasaponinⅡand human serum albumin

作　　者：桑尚源[1] 光翠娥[1] 江波[1] 

机构地区：[1]食品科学与技术国家重点实验室,江南大学,江苏无锡214122

出　　处：《食品工业科技》2016年第8期130-134,共5页Science and Technology of Food Industry

基　　金：国家自然科学基金资助项目(31201289);食品科学与技术国家重点实验室创新探索课题(SKLF-ZZA-201503)

摘　　要：为研究吸收进入人体血循环的大豆皂苷Ⅱ与人血清白蛋白(HSA)相互作用机理。采用圆二色光谱、内源荧光光谱和分子模拟方法检测表征皂苷Ⅱ与HSA之间的相互作用。圆二色光谱结果显示,大豆皂苷Ⅱ与HSA的浓度比例为1∶2或1∶4时,HSA的二级结构α螺旋含量上升,β折叠含量下降。荧光光谱显示,大豆皂苷Ⅱ对HSA的立体构象有影响。分子模拟显示它们之间的结合作用力以氢键和疏水相互作用为主,HSA与皂苷糖基链中葡萄糖醛酸基(Glc A)和鼠李糖基(Rha)部分形成氢键作用的氨基酸残基包括Glu153、Ser192、Gln196、Glu450、Asp451和Ser454等,与皂苷配基三萜烯部分形成疏水相互作用的氨基酸残基主要有Ala、Leu、Val和Trp等。Study on the interaction of the absorbed soyasaponin Ⅱ with human serum albumin（ HSA） in the circulatory system was performed. The binding of soyasaponin Ⅱ to the protein was characterized by circular dichroism spectrometry,intrinsic fluorescence spectrometry and molecular. CD spectra displayed that with the concentration ratios of 1 ∶ 2 and 1 ∶ 4, alpha helical contents of HSA increased and the beta sheet contents decreased. Fluorescence spectra showed that the 3D structure of albumin after the binding of soyasaponin Ⅱwas changed. The molecular modeling revealed that the binding forces of soyasaponin Ⅱ to HSA were mainly hydrogen bond and hydrophobic interactions. Glc A and Rha parts of soyasaponin sugar chains and amino acid residues,including Glu153,Ser192,Gln196,Glu450,Asp451 and Ser454,formed hydrogen bonds. The aglycone of soyasaponinⅡhad the hydrophobic interaction with HSA,amino acid residues of which were mainly Leu,Val,Ala and Trp.

关 键 词：大豆皂苷Ⅱ 人血清白蛋白 相互作用 圆二色光谱 分子模拟 

分 类 号：TS214.01[轻工技术与工程—粮食、油脂及植物蛋白工程]