Exploring the Inhibitory Mechanism of Piceatannol on α-glucosidase Relevant to Diabetes Mellitus

Overview

Journal RSC Adv

Publisher Royal Society of Chemistry

Specialty Chemistry

Date 2022 May 2

PMID 35495253

Authors

Lili Jiang

Zhen Wang

Xiaoyu Wang

Shujuan Wang

Jun Cao

Yong Liu

Affiliations

Soon will be listed here.

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 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.

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