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Abstract Title:

Galangin inhibitsα-glucosidase activity and formation of non-enzymatic glycation products.

Abstract Source:

Food Chem. 2019 Jan 15 ;271:70-79. Epub 2018 Jul 24. PMID: 30236734

Abstract Author(s):

Li Zeng, Huafang Ding, Xing Hu, Guowen Zhang, Deming Gong

Article Affiliation:

Li Zeng

Abstract:

Inhibition ofα-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 withthe 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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