Comparison of Flavonoid and Flavonoid Glycoside in the Inhibition of the Starch Hydrolyzing Enzymes and AGEs; A Virtual Approaches

J Oleo Sci. 2023;72(8):787-797. doi: 10.5650/jos.ess23027.

Abstract

Inhibition of α-amylase, α-glucosidase, and advanced glycation end products (AGEs) is considered a prospective method for the prevention of type II diabetes. As two flavonoids obtained from fruits, swertisin (SW) and apigenin (AP) have similar structures and display various pharmacological properties. To examine the effects of flavonoid structure on inhibition of AGEs adducts and carbohydrate hydrolyzing enzymes activity, molecular docking and molecular dynamic simulations (MDs) were used. The molecular docking method was performed by the Autodock program, and the ligand that showed the most negative binding energy was selected for further investigation. SW showed the potential ability to inhibit the AGEs formation and carbohydrate hydrolyzing enzymes activity. The stability of the receptor/SW complex was evaluated by MDs. Based on the findings of the present study, it was found that SW has the potential to reduce glycation and delay the activity of α-amylase and α-glucosidase enzymes.

Keywords: AGEs; diabetes; flavonoids; α-amylase; α-glucosidase.

Publication types

  • Comparative Study

MeSH terms

  • Carbohydrates
  • Diabetes Mellitus, Type 2* / prevention & control
  • Flavonoids* / pharmacology
  • Glycation End Products, Advanced / metabolism
  • Glycoside Hydrolase Inhibitors / chemistry
  • Glycoside Hydrolase Inhibitors / pharmacology
  • Glycosides
  • Humans
  • Molecular Docking Simulation
  • Starch
  • alpha-Amylases
  • alpha-Glucosidases / metabolism

Substances

  • alpha-Amylases
  • alpha-Glucosidases
  • Carbohydrates
  • Flavonoids
  • Glycation End Products, Advanced
  • Glycoside Hydrolase Inhibitors
  • Glycosides
  • Starch