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  • Title: Inhibitory activity of (-)-epicatechin-3,5-O-digallate on α-glucosidase and in silico analysis.
    Author: Kim JH, Kim HY, Yang SY, Kim JB, Jin CH, Kim YH.
    Journal: Int J Biol Macromol; 2018 Feb; 107(Pt A):1162-1167. PubMed ID: 28958819.
    Abstract:
    (-)-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.
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