In vitro inhibitory effects of Chinese bayberry (Myrica rubra Sieb. et Zucc.) leaves proanthocyanidins on pancreatic α-amylase and their interaction

Chinese bayberry leaves proanthocyanidins (BLPs) belongs to the prodelphinidin category with potent EGCG unit, whose inhibition effect on α-amylase and their interaction were investigated by in vitro digestion and enzyme kinetic analysis, multi fluorescence spectroscopies (fluorescence quenching, synchronous fluorescence, and three-dimensional fluorescence), circular dichroism spectra, Fourier transform infrared spectroscopy and in silico modelling. The results revealed that BLPs was a mixed inhibitor to α-amylase with the IC50 value of 3.075 ± 0.073 μg/mL. BLPs could lead to a static fluorescence quenching of α-amylase, mainly by means of interacting with amino acids (mainly Try and Tyr residues) in one site on α-amylase molecule under the action of hydrogen bonding and/or Van der Waals force. This interaction further induced the change of secondary conformational structure, functional group structure and hydrophobicity of α-amylase, thus resulting in lowering activity. Molecular docking simulated that this binding occurred in a cavity on the surface of the α-amylase molecule, and BLPs trimer showed a relatively high binding energy. The present study provided a new insight of BLPs as an α-amylase inhibitor, which could be considered in anti-diabetic therapy.