Inhibitory evaluation of Curculigo latifolia on α-glucosidase, DPP (IV) and in vitro studies in antidiabetic with molecular docking relevance to type 2 diabetes mellitus

J Enzyme Inhib Med Chem. 2021 Dec;36(1):109-121. doi: 10.1080/14756366.2020.1844680.

Abstract

The inhibition of α-glucosidase and DPP enzymes capable of effectively reducing blood glucose level in the management of type 2 diabetes. The purpose of the present study is to evaluate the inhibitory potential of α-glucosidase and DPP (IV) activity including with the 2-NBDG uptake assay and insulin secretion activities through in vitro studies. The selected of active compounds obtained from the screening of compounds by LC-MS were docked with the targeted enzyme that involved in the mechanism of T2DM. From the results, root extracts displayed a better promising outcome in α-glucosidase (IC50 2.72 ± 0.32) as compared with the fruit extracts (IC50 3.87 ± 0.32). Besides, root extracts also displayed a better activity in the inhibition of DPP (IV), enhance insulin secretion and glucose uptake activity. Molecular docking results revealing that phlorizin binds strongly with α-glucosidase, DPP (IV) and Insulin receptor (IR) enzymes with achieving the lowest binding energy value. The present work suggests several of the compounds have the potential that contribute towards inhibiting α-glucosidase and DPP (IV) and thus effective in lowering post-prandial hyperglycaemia.

Keywords: Curculigo latifolia; DPP (IV); molecular docking; type 2 diabetes; α-glucosidase.

MeSH terms

  • Animals
  • Cell Survival / drug effects
  • Cells, Cultured
  • Curculigo / chemistry*
  • Diabetes Mellitus, Type 2 / drug therapy*
  • Diabetes Mellitus, Type 2 / metabolism
  • Dipeptidyl Peptidase 4 / metabolism
  • Dipeptidyl-Peptidase IV Inhibitors / chemistry
  • Dipeptidyl-Peptidase IV Inhibitors / isolation & purification
  • Dipeptidyl-Peptidase IV Inhibitors / pharmacology*
  • Dose-Response Relationship, Drug
  • Fruit / chemistry
  • Glycoside Hydrolase Inhibitors / chemistry
  • Glycoside Hydrolase Inhibitors / isolation & purification
  • Glycoside Hydrolase Inhibitors / pharmacology*
  • Hypoglycemic Agents / chemistry
  • Hypoglycemic Agents / isolation & purification
  • Hypoglycemic Agents / pharmacology*
  • Insulin Secretion
  • Mice
  • Molecular Docking Simulation
  • Molecular Structure
  • Plant Extracts / chemistry
  • Plant Extracts / isolation & purification
  • Plant Extracts / pharmacology*
  • Rats
  • Structure-Activity Relationship
  • alpha-Glucosidases / metabolism

Substances

  • Dipeptidyl-Peptidase IV Inhibitors
  • Glycoside Hydrolase Inhibitors
  • Hypoglycemic Agents
  • Plant Extracts
  • alpha-Glucosidases
  • Dipeptidyl Peptidase 4

Grants and funding

This work was funding by Putra Graduate Initiative Grant (GP-IPS) under vote number [9645100], Universiti Putra Malaysia (UPM).