化学
疏水效应
色氨酸
活动站点
氢键
对接(动物)
猝灭(荧光)
淀粉酶
结合位点
荧光光谱法
立体化学
酶
荧光
生物物理学
结晶学
氨基酸
生物化学
有机化学
分子
医学
物理
护理部
量子力学
生物
作者
Yanyi Huang,Samantha J. Richardson,Charles S. Brennan,Stefan Kasapis
标识
DOI:10.1016/j.foodhyd.2023.109467
摘要
The inhibitory mechanism of gallic acid (GA) on α-amylase was investigated through enzymatic inhibition assays, multi-spectroscopy, Job plot analysis and in-silico molecular docking. The results reveal that GA competitively binds to the active site of α-amylase in a 1:1 stoichiometry, dominantly via four hydrogen bonds and one hydrophobic interaction. The α-amylase-GA complex showed an increased thermal stabilisation, accompanied by a rise in α-helical and β-sheet components, resulting in a partial folding of the protein structure. The compact structure prevents substrate binding and inhibits enzyme activity. The self-quenching ability of GA was considered in the intrinsic fluorescence analysis, revealing a distinct loss in fluorescence intensity with a blueshift in the α-amylase-GA complex spectra. This observation suggests a direct interaction between GA and tryptophan amino acid residues, as the residues move to a more hydrophobic environment. Findings in this study provide insights into the interaction mechanism between GA and α-amylase, which will aid in understanding the inhibitory mechanism of their complex forms found in nature.
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