(-)-Epicatechin-3,5-O-digallate (ECDG) from Orostachys japonicus A. Berger was examined for inhibitory activity on α-glucosidase. The results showed that the IC50 value was achieved with nanomolar concentrations. Through the enzyme kinetic analysis, ECDG was shown to act as a competitive inhibitor of α-glucosidase by binding to the receptor active site. Fluorescence-quenching measurements showed that ECDG and the enzyme may have a one-to-one reaction with low quenching (Ksv) and binding constants. A molecular docking study was performed to evaluate the receptor-ligand complex. Asn236 was found to be particularly important for hydrogen bond formation during the molecular dynamics simulation.
Keywords: Competitive inhibitor; Epicatechin derivative; Molecular docking; Molecular dynamics; α-Glucosidase.
Copyright © 2017. Published by Elsevier B.V.