茶黄素-3,3’-双没食子酸酯对α-葡萄糖苷酶的抑制机制  被引量:2

Inhibitory Mechanism of Theaflavin-3,3’-digallate onα-Glucosidase

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作  者:曹宇凡 黄伟[1] 陈取明 蔡为荣[1] CAO Yufan;HUANG Wei;CHEN Quming;CAI Weirong(College of Biological and Food Engineering,Anhui Polytechnic University,Wuhu 241000,China)

机构地区:[1]安徽工程大学生物与食品工程学院,安徽芜湖241000

出  处:《食品科学》2024年第21期104-111,共8页Food Science

基  金:安徽省重点研发计划项目(202004a06020022)。

摘  要:利用酶抑制动力学、多光谱、分子对接分析了茶黄素-3,3’-双没食子酸酯(theaflavin-3,3’-digallate,TFDG)对α-葡萄糖苷酶的抑制机制,结果表明抑制是可逆的,并呈现竞争型和非竞争型混合抑制;TFDG与α-葡萄糖苷酶形成复合物猝灭其固有荧光;热力学参数表明结合是自发吸热、熵增的,且疏水相互作用是主要驱动力;结合增强了酪氨酸残基附近的疏水性和色氨酸残基周围的极性,降低了α-螺旋、β-折叠和β-转折的含量。分子对接显示TFDG结合在酶活性位点附近,并与附近氨基酸残基Phe450、Trp406之间存在两种疏水相互作用,且与Asp203、Phe450、Gln603形成3个氢键。本研究揭示了TFDG抑制α-葡萄糖苷酶的分子机理,为治疗糖尿病提供一种可行的候选功能因子。The mechanism ofα-glucosidase inhibition by theaflavin-3,3’-digallate(TFDG)was analyzed using enzyme inhibition kinetics,multi-spectroscopies and molecular docking.The results indicated that the inhibition was reversible and displayed a mixed type of competitive and non-competitive inhibition.TFDG quenched the intrinsic fluorescence ofα-glucosidase by forming a complex with it.Thermodynamic parameters suggested that the binding was a spontaneous,endothermic and entropy-increasing process,mainly driven by hydrophobic interactions.The binding enhanced the hydrophobicity near Tyr residue and the polarity around Trp residue,reducing the contents ofα-helix,β-sheet andβ-turn.Molecular docking revealed that TFDG bound in close proximity to the enzyme’s active site,engaging in two hydrophobic interactions with Phe450 and Trp406 residues,respectively,as well as forming three hydrogen bonds with amino acid residues Asp203,Phe450 and Gln603,respectively.This study provides evidence for the potential of TFDG as a feasible candidate functional factor for the treatment of diabetes.

关 键 词:茶黄素-3 3′-双没食子酸酯 Α-葡萄糖苷酶 抑制机制 多光谱 分子对接 

分 类 号:TS201.2[轻工技术与工程—食品科学]

 

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