Abstract

1,2,3,4,6-Penta-O-galloyl-β-D-glucopyranose (β-PGG) is a compound commonly available in vegetables and fruits. It exhibited potential inhibition of α-glucosidase and hypoglycemic effect in vivo. This study explored its dynamics properties inhibiting α-glucosidase by Lineweaver − Burk plots, spectral analysis, docking analysis, and molecular dynamics simulations. β-PGG showed a mix-type inhibition when it was interacting with α-glucosidase. The fluorescence quenching indicated that the PGG-glucosidase complex formed in a spontaneous exothermic process and was driven by enthalpy. The synchronous fluorescence and ECD spectra indicate that β-PGG induced and changed the enzyme conformation in the complex formation. Docking results revealed multiple hydrogen bonds between the phenols and the amino acid residues. Further dynamic simulations indicated that the residues Asp345, Phe153, Arg435, Glu300, Pro305, and Phe296 played a more critical role in the interactions between β-PGG and α-glucosidase.

摘要

1,2,3,4,6-Penta-O-galloyl-β-D-吡喃葡萄糖 (β-PGG) 是一种常见于蔬菜和水果中的化合物。它在体内表现出潜在的α-葡萄糖苷酶抑制和降血糖作用. 本研究通过 Lineweaver - Burk 图、光谱分析、对接分析和分子动力学模拟探索了其抑制 α-葡萄糖苷酶的动力学特性。β-PGG与α-葡萄糖苷酶相互作用时表现出混合型抑制。荧光猝灭表明PGG-葡萄糖苷酶复合物在自发放热过程中形成并且由焓驱动。同步荧光和ECD光谱表明β-PGG诱导并改变了复合物形成中的酶构象。对接结果显示酚类和氨基酸残基之间存在多个氢键。进一步的动态模拟表明残基 Asp345、Phe153、Arg435、Glu300、Pro305 和 Phe296 在 β-PGG 和 α-葡萄糖苷酶之间的相互作用中起更关键的作用。