Inhibitory Mechanism of Taxifolin against α-Glucosidase Based on Spectrofluorimetry and Molecular Docking

Abstract

The α-glucosidase inhibitory activity and behavior of taxifolin was first investigated by spectrofluorimetry and molecular docking. It was found that taxifolin inhibits α-glucosidase in a competitive manner with the IC 50 value of 0.16 mg/mL. The intrinsic fluorescence quenching of α-glucosidase in the presence of taxifolin was observed by the static quenching mechanism. According to the thermodynamic study, the complex of taxifolin and α-glucosidase was maintained by van der Waals and hydrogen bonding. The binding mode provided by molecular docking simulation indicated the existence of hydrogen bonding between taxifolin and the amino acid residues of α-glucosidase (Glu429, Asp 568 and Glu771), which coincided with the result of fluorescence analysis.

Preparation and α-Glucosidase Inhibitory Activity of Gallic Acid-Dextran Conjugate

“…16 However, low-molecular-weight polyphenols (such as flavonoids and phenolic acids) are usually competitive α-glucosidase inhibitors. 17,18 The above results indicated the mechanism as follows: Dextran (average molecular weight <1000) has good water solubility. When it is connected with gallic acid by ester bonds, its hydrophobicity can be significantly improved.…”

Insights into the Pharmacological Effects of Flavonoids: The Systematic Review of Computer Modeling

“…Molecular docking has the greatest prevalence, which was used in 92.4% of the analyzed articles [ 34 , 35 , 36 , 37 , 38 , 39 ]. Molecular dynamics simulations were revealed in 31.8% of the papers [ 40 , 41 , 42 , 43 ].…”

Inhibitory activity of flavonoids against human sucrase-isomaltase (α-glucosidase) activity in a Caco-2/TC7 cellular model

“…20,36–38 Taxifolin has also shown promising inhibitory activity against α-glucosidase from Saccharomyces cerevisiae . 39…”