Exploring the inhibitory mechanism of piceatannol on α-glucosidase relevant to diabetes mellitus.

ABSTRACT: Due to their association with type 2 diabetes mellitus treatment, α-glucosidase inhibitors have attracted increasing attention of researchers. In this study, we systemically investigated the kinetics and inhibition mechanism of piceatannol on α-glucosidase. Enzyme kinetics analyses showed that piceatannol exhibited strong inhibition on α-glucosidase in a non-competitive manner. Spectroscopy analyses indicated that piceatannol could bind with α-glucosidase to form complexes via high affinity. Further, computational molecular dynamics and molecular docking studies validated that the binding of piceatannol was outside the catalytic site of α-glucosidase, which would induce conformational changes of α-glucosidase and block the entrance of substrate, causing declines in α-glucosidase activities. Our results provide useful information not only for the inhibition mechanism of piceatannol against α-glucosidase but also for a novel target site for developing novel α-glucosidase inhibitors as potential therapeutic agents in the treatment of type 2 diabetes mellitus.

SUBMITTER: Jiang L 

PROVIDER: S-EPMC9049079 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature