化学
糖基化
生物化学
糖基化
酪氨酸
色氨酸
酶
原花青素
作用机理
抑制性突触后电位
极性(国际关系)
活动站点
立体化学
多酚
类黄酮
结合位点
碳水化合物
非共价相互作用
丹宁
生物活性
生物物理学
非竞争性抑制
转移酶
疏水效应
酶抑制
结构-活动关系
作者
Shanmei Zeng,Wu-Mei Jiang,Yan Lin,Ze-Lin Liao,Jiayi Liang,Ze-Dan Yang,Wen-Jing Wu,Jia-Yi Luo,Wei‐Ming Chai
标识
DOI:10.1021/acs.jafc.5c14159
摘要
. Inhibitory mechanism analyses showed that the combination of HLCTs to α-glucosidase was propelled by noncovalent interactions, which modified the polarity and hydrophobicity near tyrosine and tryptophan residues in the binding site and induced variation of the enzyme's secondary structure and conformation, leading to an inhibition of enzyme activity. In addition, HLCTs effectively inhibited nonenzymatic glycosylation by reducing glycosylation products, protein carbonylation, protein oxidation, and amyloid cross-β structures. These findings provided a scientific basis for the application of HLCTs as potential type 2 diabetes drugs.
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