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 Phe 77 and Asp 79 . 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.