葛根素对α-糜蛋白酶的结构及其活性影响  

Effect of Puerarin on the Structure and Activity ofα-Chymotrypsin

作　　者：田建袅[1,2] 黎彩凤[2] 赵彦春[2] 周柳金[2] 赵书林[1,2] 

机构地区：[1]药用资源化学与分子工程教育部重点实验室,桂林541004 [2]广西师范大学化学化工学院,桂林541004

出　　处：《理化检验（化学分册）》2010年第4期364-367,共4页Physical Testing and Chemical Analysis(Part B:Chemical Analysis)

基　　金：国家自然科学基金(2006088);广西应用基础研究专项(0639028);广西师范大学重点项目(师政科技2005第1号)资助

摘　　要：应用荧光光谱、圆二色光谱及酶活性检测等方法研究了葛根素与α-糜蛋白酶的相互作用,结果表明:葛根素对α-糜蛋白酶的荧光猝灭机理为非辐射能量转移的静态猝灭,两者之间的相互作用力主要是范德华力或氢键作用力,根据F(o|¨)rster非辐射能量转移理论测得葛根素在α-糜蛋白酶中的结合位置与色氨酸残基间的距离为3.67 nm;通过圆二色谱(CD)光谱研究表明葛根素能够引起α-糜蛋白酶的二级结构发生变化;酶活性试验表明葛根素可作为α-糜蛋白酶的抑制剂。The interaction of puerarin andα-chymotrypsin was studied by fluorescence spectrometry,circular dichrosim spectrometry and measurement of enzyme activity.It was found that the mechanism of fluorescence quenching ofα-chymotrypsin by puerarin was a static quenching of non-radiative energy transfer,and that the interaction between them was mainly related to the action of van der Waals forces or hydrogen bond.Distance between the binding position of puerarin inα-chymotrypsin and the tryptophan radical was calculated by the Foerster non-radiative energy transfer theory and found to be 3.67 nm.Besides,change of secondary structure ofα-chymotrypsin was induced by pueparin as shown by the result of circular dichroism spectroscopic study,and pueparin was capable to be used as an inhibitor for activity ofα-chymotrypsin.

关 键 词：葛根素 Α-糜蛋白酶 荧光光谱 圆二色谱 酶活性 

分 类 号：O657[理学—分析化学]