Insight into the α-glucosidase-inhibiting mechanism of β-PGG, a commonly occurring polyphenol in diets

• Published in: Natural product research Vol. 36; no. 5; pp. 1380 - 1384
• Main Authors: Huang, Cheng-Di, Zheng, Hang-Hang, Zhang, Xiao-Yue, Liu, Da-Zhi, Gao, Jin-Ming, Zhang, Qiang
• Format: Journal Article
• Language: English
• Published: England 04-03-2022
• Subjects: alpha-Glucosidases - metabolism; Diet; Hydrolyzable Tannins - pharmacology; Molecular Docking Simulation; Polyphenols; inhibition mechanism; α-glucosidase; diet; dynamic simulation; β-PGG
• ISSN: 1478-6419; 1478-6427
• DOI: 10.1080/14786419.2021.1873983

1,2,3,4,6-Penta-O-galloyl-β-D-glucopyranose (β-PGG) is a compound commonly available in vegetables and fruits. It exhibited potential inhibition of α-glucosidase and hypoglycemic effect in
. This study explored its dynamics properties inhibiting α-glucosidase by Lineweaver - Burk plots, spectral analysis, docking analysis, and molecular dynamics simulations. β-PGG showed a mix-type inhibition when it was interacting with α-glucosidase. The fluorescence quenching indicated that the PGG-glucosidase complex formed in a spontaneous exothermic process and was driven by enthalpy. The synchronous fluorescence and ECD spectra indicate that β-PGG induced and changed the enzyme conformation in the complex formation. Docking results revealed multiple hydrogen bonds between the phenols and the amino acid residues. Further dynamic simulations indicated that the residues Asp345, Phe153, Arg435, Glu300, Pro305, and Phe296 played a more critical role in the interactions between β-PGG and α-glucosidase.