Exploring the inhibitory mechanism of piceatannol on α-glucosidase relevant to diabetes mellitus
Lili Jiang, Zhen Wang, Xiaoyu Wang, Shujuan Wang, Jun Cao, Yong Liu
Abstract
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.
Topics & Concepts
PiceatannolChemistryAcarboseType 2 Diabetes MellitusMechanism (biology)Non-competitive inhibitionEnzymeKineticsDiabetes mellitusPharmacologyBiochemistryStereochemistryMedicineResveratrolEndocrinologyPhilosophyQuantum mechanicsPhysicsEpistemologyNatural Antidiabetic Agents StudiesPhytochemicals and Antioxidant ActivitiesAdvanced Glycation End Products research