Structural changes and molecular mechanism study on the inhibitory activity of epigallocatechin against α-glucosidase and α-amylase.

ABSTRACT: In this study, the inhibition and mechanism of epigallocatechin (EGC) on two key glycoside hydrolases (α-glucosidase, α-amylase) were explored from the molecular structure level. The chemical structure of EGC was characterized by X-ray diffraction, Fourier transform infrared (FTIR) spectroscopy, and proton nuclear magnetic resonance spectroscopy. EGC's inhibition on these enzymes was colorimetrically determined. The effects of EGC on the chemical structure and spatial configuration of the enzymes were explored via FTIR spectroscopy, fluorescence spectroscopy, and molecular docking techniques. The results showed that EGC exhibited the inhibition of α-glucosidase and α-amylase in a non-competitive manner, showing a continuous upward trend as EGC's concentration increased. There was a

SUBMITTER: Man Z 

PROVIDER: S-EPMC9682078 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature