Journal
FOOD CHEMISTRY
Volume 271, Issue -, Pages 70-79Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2018.07.148
Keywords
alpha-Glucosidase; Non-enzymatic glycation; Galangin; Mechanism of alpha-glucosidase inhibition
Funding
- National Natural Science Foundation of China [31460422, 31060210]
- Natural Science Foundation of Jiangxi Province, China [20171BAB204029, 20143ACB20006]
- Project of Science and Technology of Jiangxi Provincial Education Department, China [GJJ150187]
- Research Project of State Key Laboratory of Food Science and Technology [SKLF-ZZB-201707, SKLF-ZZA-201612, SKLF-KF-201607]
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Inhibition of alpha-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 alpha-glucosidase and non-enzymatic glycation. Galangin showed a reversible inhibition on a-glucosidase activity in a mixed-type manner through a monophasic kinetic process, and induced the fluorescence quenching and conformational changes of alpha-glucosidase by forming alpha-glucosidase-galgangin complex. Molecular docking revealed that galangin primarily interacted with the amino acid residues within the active site of alpha-glucosidase, which may prevent the entrance of substrate resulting in a decrease in catalytic efficiency of alpha-glucosidase. Moreover, galangin moderately inhibited the formation of intermediates of non-enzymatic glycation, fructosamine and alpha-dicarbonyl compounds and strongly inhibited the formation of advanced glycation end products.
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