Insight into the binding characteristics of epigallocatechin-3-O-gallate and alcohol dehydrogenase: Based on the spectroscopic and molecular docking analysis

化学 对接(动物) 醇脱氢酶 氢键 没食子酸 没食子酸表没食子酸酯 乙醇 立体化学 生物化学 生物物理学 分子 有机化学 多酚 抗氧化剂 核化学 生物 医学 护理部
作者
Xiaodan Zhang,Lili Liu,Yuantu Wang,Ying Yu,Weiwei Cheng,Baocheng Xu,Feng Xiao
出处
期刊:Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy [Elsevier BV]
卷期号:310: 123943-123943 被引量:8
标识
DOI:10.1016/j.saa.2024.123943
摘要

Alcohol dehydrogenase (ADH) is one of the pivotal enzymes for alcohol metabolism, which plays an important role in many physiological processes. In this study, the activation effects of epigallocatechin-3-O-gallate (EGCG) on ADH and the characteristics of the interaction were investigated via biochemical method, spectroscopy methods, and molecular docking. The results demonstrated that EGCG significantly increased the catalytic activity of ADH with a 33.33% activation rate and that EGCG blending slightly altered the microenvironment surrounding ADH aromatic amino acids, with an increase in the quantity of β-sheet and a decrease in the α-helix. Through the thermal stability analysis, it is further shown that the interaction of the two affects the intra-molecular hydrogen bond formation of the protein, and the conformation is partially extended. Besides, a total of 8 residues in ADH participated in the docking with EGCG, among which Asp-227, Lys-231, Glu-234, Gly-365 and Glu-366 participated in the formation of hydrogen bonds. At the same time, EGCG and amino group of Lys-231 form a noncovalent bond through cation-π interaction. In particular, hydrogen bonding was beneficial to keep the stability of EGCG-ADH, which was the primary driver of ADH activity activation. The results supply a new way for EGCG to activate ADH and a theoretical basis for the development of anti-alcoholism products.
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