Identification and molecular docking study of sugarcane leaf-derived compounds as potent dipeptidyl peptidase IV, α-glucosidase, and α-amylase inhibitors

J Sci Food Agric. 2023 Aug 30;103(11):5388-5400. doi: 10.1002/jsfa.12613. Epub 2023 May 21.

Abstract

Background: Dipeptidyl peptidase-IV (DPP-IV), α-glucosidase, and α-amylase play a prominent role in regulating postprandial blood sugar levels, which are regarded as key targets for the treatment of type 2 diabetes mellitus (T2DM). The present study aimed to characterize bioactive compounds as potent crucial sugar metabolism enzyme inhibitors from sugarcane leaves by virtual screening. In total, 41 sugarcane leaf-derived compounds were used for the screening of multiple targets. Subsequently, the molecular mechanism and activity validation in vitro of the interaction between enzymes and compound were carried out.

Results: Flavonoid compound schaftoside was identified by molecular simulation and showed significant DPP-IV (0.1050 ± 1.22 mmol L-1 ), α-glucosidase (0.078 ± 0.06 mmol L-1 ), and α-amylase (0.3067 ± 0.35 mmol L-1 ) inhibitory effects. The residues ARG125 and TYR662 of DPP-IV may play crucial roles in inhibiting the activity of DPP-IV. Multiple hydrogen bonds and electrostatic interactions were exhibited between schaftoside and α-glucosidase. Molecular modeling revealed that schaftoside displays strong binding with the catalytic triad (ASP197, ASP300, and GLU233) of α-amylase.

Conclusion: Our findings demonstrate that schaftoside from sugarcane leaves might be an edible for T2DM treatment." © 2023 Society of Chemical Industry.

Keywords: DPP-IV; schaftoside; sugarcane leaves; type 2 diabetes mellitus; α-amylase; α-glucosidase.

Publication types

  • Review

MeSH terms

  • Diabetes Mellitus, Type 2* / drug therapy
  • Dipeptidyl Peptidase 4 / chemistry
  • Dipeptidyl-Peptidase IV Inhibitors* / chemistry
  • Dipeptidyl-Peptidase IV Inhibitors* / pharmacology
  • Glycoside Hydrolase Inhibitors / chemistry
  • Humans
  • Hypoglycemic Agents / chemistry
  • Hypoglycemic Agents / pharmacology
  • Molecular Docking Simulation
  • Plant Leaves / metabolism
  • Saccharum* / metabolism
  • alpha-Amylases / chemistry
  • alpha-Glucosidases / chemistry

Substances

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