高良姜素
化学
糖基化
甲基乙二醛
生物化学
酶
槲皮素
抗氧化剂
受体
山奈酚
作者
Li Zeng,Huafang Ding,Xing Hu,Guowen Zhang,Deming Gong
出处
期刊:Food Chemistry
[Elsevier BV]
日期:2018-07-24
卷期号:271: 70-79
被引量:186
标识
DOI:10.1016/j.foodchem.2018.07.148
摘要
Inhibition of α-glucosidase and non-enzymatic glycation is considered as an effective approach to treat type 2 diabetes. Herein, multispectroscopic techniques and molecular docking analysis were used to investigate the inhibition of galangin on α-glucosidase and non-enzymatic glycation. Galangin showed a reversible inhibition on α-glucosidase activity in a mixed-type manner through a monophasic kinetic process, and induced the fluorescence quenching and conformational changes of α-glucosidase by forming α-glucosidase-galgangin complex. Molecular docking revealed that galangin primarily interacted with the amino acid residues within the active site of α-glucosidase, which may prevent the entrance of substrate resulting in a decrease in catalytic efficiency of α-glucosidase. Moreover, galangin moderately inhibited the formation of intermediates of non-enzymatic glycation, fructosamine and α-dicarbonyl compounds and strongly inhibited the formation of advanced glycation end products.
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