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

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.