期刊
BIOORGANIC CHEMISTRY
卷 101, 期 -, 页码 -出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bioorg.2020.104029
关键词
Bayberry leaves proanthocyanidins (BLPs); alpha-Amylase; Interaction mechanism
资金
- Ningxia Key Research and Development Program [2018BBF02010]
Chinese bayberry leaves proanthocyanidins (BLPs) belongs to the prodelphinidin category with potent EGCG unit, whose inhibition effect on alpha-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 alpha-amylase with the IC50 value of 3.075 +/- 0.073 mu g/mL. BLPs could lead to a static fluorescence quenching of alpha-amylase, mainly by means of interacting with amino acids (mainly Try and Tyr residues) in one site on alpha-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 alpha-amylase, thus resulting in lowering activity. Molecular docking simulated that this binding occurred in a cavity on the surface of the alpha-amylase molecule, and BLPs trimer showed a relatively high binding energy. The present study provided a new insight of BLPs as an alpha-amylase inhibitor, which could be considered in anti-diabetic therapy.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据