Antidiabetic and antiparasitic potentials: Inhibition effects of some natural antioxidant compounds on α-glycosidase, α-amylase and human glutathione S-transferase enzymes

Int J Biol Macromol. 2018 Nov:119:741-746. doi: 10.1016/j.ijbiomac.2018.08.001. Epub 2018 Aug 1.

Abstract

The glutathione S-transferase (GST) was purified from fresh blood erythrocytes using affinity column chromatography. Also, α-amylase from porcine pancreas and α-glycosidase from Saccharomyces cerevisiae were used as target enzymes. In this study, these compounds were tested on α-amylase, α-glycosidase, and GST enzymes and demonstrated effective inhibitor compounds with Ki values in the range of 8.34-40.78 μM against GST, and 120.53-892.36 nM against α-glycosidase. Additionally, the phenolic molecules were tested for the inhibition of α-amylase enzyme which determined effective inhibition profile with IC50 values in the range of 175.01-626.58 nM. Indeed, these molecules can be elective inhibitors of GST, α-glycosidase and α-amylase enzymes as antidiabetic and antiparasitic agents.

Keywords: Antidiabetic; Antiparasitic; Enzyme inhibition; Glutathione S-transferase.

MeSH terms

  • Antioxidants / pharmacology*
  • Antiparasitic Agents / pharmacology*
  • Glutathione Transferase / antagonists & inhibitors*
  • Glycoside Hydrolase Inhibitors / pharmacology*
  • Humans
  • Hypoglycemic Agents / pharmacology*
  • Molecular Structure
  • Reactive Oxygen Species / metabolism
  • alpha-Amylases / antagonists & inhibitors*
  • alpha-Glucosidases / metabolism*

Substances

  • Antioxidants
  • Antiparasitic Agents
  • Glycoside Hydrolase Inhibitors
  • Hypoglycemic Agents
  • Reactive Oxygen Species
  • Glutathione Transferase
  • alpha-Amylases
  • alpha-Glucosidases