芹菜素抑制α-葡萄糖苷酶的分子机制研究  

Study on the molecular inhibition mechanisms of apigenin on α-glucosidase

作　　者：屠洁[1,2] 陈钧[1] 刘冠卉[2] 

机构地区：[1]江苏大学食品与生物工程学院,江苏镇江212013 [2]江苏科技大学生物技术学院,江苏镇江212018

出　　处：《生物技术》2015年第4期369-374,共6页Biotechnology

摘　　要：[目的]分析芹菜素对α-葡萄糖苷酶的抑制作用类型,并探讨其抑制的分子作用机制。[方法]采用Lineweaver-Burk双倒数方程,分析芹菜素对α-葡萄糖苷酶的抑制作用类型;荧光光谱和分子对接阐述芹菜素抑制α-葡萄糖苷酶的分子作用机制。[结果]芹菜素对α-葡萄糖苷酶的抑制类型为竞争型抑制,抑制常数Ki=12.08μg/m L。芹菜素和α-葡萄糖苷酶的结合导致酶分子的内在荧光静态猝灭,不同温度(298 K、304 K、310 K)条件下荧光猝灭常数KA分别为0.859 4×104、0.617 7×104、0.486 5×104L/mol。酶分子中Tyr158、Ser240、Pro312、Phe314和Asn415等氨基酸残基为芹菜素与其结合的重要活性位点,芹菜素的A环5-OH和7-OH、B环4'-OH结构对其抑制活性起到关键作用。[结论]芹菜素是α-葡萄糖苷酶的竞争性抑制剂,疏水作用力和氢键是其与酶分子间的主要作用力。[Objective]To investigated the inhibition type of apigenin on ot - glucosidase and the inhibition molecular mecha- nisms. [ Methods] Lineweaver- Burk plot were used to study the inhibition type of apigenin on α-glucosidase, fluorescence spectroscopy along with molecular docking technique were used to study the molecular inhibition mechanisms of apigenin on α -glucosidase. [ Results] α- Glucosidase was competitively inhibited by apigenin,the inhibition constants Ki were 12.08μg/ mL. The intrinsic fluorescence of α - glucosidase was quenched by apigenin through a static quenching procedure, which was caused by their combination. The quenching constants between apigenin and α -glucosidase were 0. 859 4×10^4 L/mol （298 K） ,0.617 7×10^4 L/mol（304 K） ,0. 486 5×10^4 L/mol（310 K）. Tyr158, Ser240 ,Pro312 ,Phe314 and Asn415 in α -glucosi- dase were especially important binding site with apigenin, and the A ring 5 - OH, 7 - OH and B ring 4＇ - OH were the key groups in apigenin. [ Conclusion] Apigenin was a competitive inhibitor of α - glucosidase, and the hydrophobie interaction and hydrogen bond were main forces between apigenin and α - glueosidase.

关 键 词：芹菜素 Α-葡萄糖苷酶 荧光光谱 分子对接 抑制机制 

分 类 号：TS201.2[轻工技术与工程—食品科学]