Synthesis, α-Glucosidase inhibition and molecular docking studies of tyrosol derivatives

Nat Prod Res. 2021 May;35(10):1596-1604. doi: 10.1080/14786419.2019.1628750. Epub 2019 Jun 17.

Abstract

To find a potent α-glucosidase inhibitor, 24 tyrosol derivatives with different substituents located at the meta, ortho, or para position of the phenyl group have been synthesised via the Mitsunobu reaction, characterised by 1H NMR, 13C NMR, ESI-MS and IR and evaluated for inhibition. The derivatives possessed varying degrees of in vitro inhibitory activity against α-glucosidase and a relationship between the structure and activity was subsequently established for all compounds. Two of these compounds with substituents at the para position showed significant inhibitory effects surpassing that of the control standard acarbose. Molecular docking studies performed to better understand the binding interactions between the enzyme and the two most active compounds showed substantial binding within the active site of α-glucosidase. Taken together, these results indicate that the position of the substituent plays a crucial role in this inhibition and may facilitate the development of new α-glucosidase inhibitors.

Keywords: molecular docking; structure activity relationship; synthesis; tyrosol; α-glucosidase.

MeSH terms

  • Acarbose / chemistry
  • Acarbose / pharmacology
  • Binding Sites
  • Catalytic Domain
  • Glycoside Hydrolase Inhibitors / chemistry
  • Glycoside Hydrolase Inhibitors / pharmacology*
  • Molecular Docking Simulation*
  • Phenylethyl Alcohol / analogs & derivatives*
  • Phenylethyl Alcohol / chemical synthesis
  • Phenylethyl Alcohol / chemistry
  • Phenylethyl Alcohol / pharmacology
  • Structure-Activity Relationship
  • Yeasts / enzymology
  • alpha-Glucosidases / chemistry
  • alpha-Glucosidases / metabolism*

Substances

  • Glycoside Hydrolase Inhibitors
  • 4-hydroxyphenylethanol
  • alpha-Glucosidases
  • Phenylethyl Alcohol
  • Acarbose