Lipase activity inhibited by aloenin A: Glycoside from Aloe vera (L.) Burm. f.-In vitro and molecular docking studies

J Mol Recognit. 2023 Feb;36(2):e3002. doi: 10.1002/jmr.3002. Epub 2022 Dec 14.

Abstract

Obesity is taking over many parts of the world and has been identified as the second leading cause of preventable death, with a dramatic increase in prevalence over the last two decades. Pancreatic lipase is a lipid-digesting enzyme that plays an important role in fat metabolism. Inhibiting pancreatic lipase is an attractive target for obesity treatment. Phytochemicals or bioactive compounds/extracts isolated from medicinal plants offer a promising platform for the development of pancreatic lipase inhibitors. This study aims to characterize and investigate the effect of aloenin A, glycoside found in Aloe vera, as a possible inhibitor of pancreatic lipase in vitro and in silico. A. vera extract had an IC50 value of 0.5472 μg/ml, whereas aloenin A had an IC50 value of 14.95 μg/mL and was found to inhibit in a competitive manner. These findings were supported by molecular docking studies, which revealed that aloenin A binds to the substrate binding site with a binding energy of - 7.16 kcal/mol, and this binding site is stabilized by three hydrogen bonds contributed by Phe77 and Asp79 . Our findings suggest that the anti-hyperlipidemic effects of A. vera on pancreatic lipase can be attributed in part to the presence of aloenin A.

Keywords: Aloe vera; aloenin A; enzyme kinetics; lipid metabolism; molecular docking; obesity; pancreatic lipase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aloe* / chemistry
  • Glycosides*
  • Lipase
  • Molecular Docking Simulation
  • Plant Extracts / chemistry
  • Plant Extracts / pharmacology

Substances

  • aloenin
  • Glycosides
  • Lipase
  • Plant Extracts