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- W4200202968 abstract "Malvidin-3-O-galactoside (M3G) is known to lower blood sugar levels and enhance glucose uptake; however, the underlying mechanism remains unclear. Here, we aimed to elucidate the mechanism underlying the inhibitory effects of M3G on protein tyrosine phosphatase 1B (PTP1B) and α-glucosidase using enzyme kinetic analysis, circular dichroism spectroscopy, fluorescence quenching, and molecular docking. The results showed that M3G strongly inhibited PTP1B and α-glucosidase through reversible mixed inhibition and reversible non-competitive inhibition, respectively. M3G binding altered the secondary structures of PTP1B and α-glucosidase and regulated the microenvironment of specific amino acid residues. Additionally, different M3G concentrations quenched the intrinsic fluorescence of PTP1B/α-glucosidase. Thermodynamic studies revealed that M3G binding to PTP1B and α-glucosidase was spontaneous, whereas molecular docking analysis provided information on the interaction between M3G and PTP1B/α-glucosidase amino acid residues. These findings clarified that M3G effectively inhibited PTP1B/α-glucosidase and highlighted its role as a functional food ingredient for regulating type 2 diabetes." @default.
- W4200202968 created "2021-12-31" @default.
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- W4200202968 date "2022-04-01" @default.
- W4200202968 modified "2023-10-01" @default.
- W4200202968 title "Mechanism underlying the interaction of malvidin-3-O-galactoside with protein tyrosine phosphatase-1B and α-glucosidase" @default.
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- W4200202968 doi "https://doi.org/10.1016/j.molstruc.2021.132249" @default.
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