The in vitro and in silico investigations on the α-amylase inhibitor derived from Leptadenia lanceolata (Poir.) Goyder leaf extract

Nat Prod Res. 2024 Oct 13:1-11. doi: 10.1080/14786419.2024.2413036. Online ahead of print.

Abstract

An attempt has been made to assess the α-amylase inhibitory activity of a phytochemical compound extracted and purified from the leaf extract of Leptadenia lanceolata. The total yield of the crude leaf extract was 11.42% and among the different solvents involved in this study, hexane and ethyl acetate at 7:3 was effective in the separation of phytochemical compounds. Hexane and ethyl acetate at 25:75% ratios (elution S4) were found greater in inhibiting α-amylase enzyme (83%). The most abundant compound found was Phytol (3,7,11,15-tetramethyl-2-hexadecen-1-ol) and its derivatives. It resulted that the binding energy for acarbose and phytol were -8.1 kcal/mol and -5.9 kcal/mol respectively. However, the binding affinity was greater in the case of acarbose than phytol and the binding sites are different for both the ligands. Therefore, this study adds scientific evidence of the α-amylase inhibitory activity of phytol derived from the leaf extract of L. lanceolata.

Keywords: FT-IR; GC-MS; Leptadenia lanceolata; inhibition; molecular docking; phytol; α-amylase.