Title : Targeting alzheimer’s proteins: Binding and pharmacokinetics of Mimosa pudica leaf extracts
Abstract:
This study revealed the bioactive volatile components of Mimosa pudica leaf hydro-ethanol extract using gas chromatography-mass spectrometry (GC-MS) and investigated the computational binding characteristics with β-Site APP-cleaving enzyme (BACE 1). Pharmacokinetic properties of the volatile components were also investigated using ADMET properties. Molecular docking and pharmacokinetic studies of the volatile compounds were evaluated using docking software Auto Dock Vina, and SwissADME respectively. GC-MS analysis revealed forty-three (43) compounds which showed distinct binding affinities with BACE 1. The affinities ranged from –5.0 to – 9.6 kcal/mol; 1-methyl-4-[(2Z)-6-methylhepta-2,5-dien-2-yl]-7-oxabicyclo [4.1.0] heptane and 3,6,6-trimethyl-1-phthalazin-1-yl-1,5,6,7-tetrahydro-Indazol-4-one presented the highest binding affinity of -7.9 and – 9.6 kcal/mol respectively. The binding affinities of extracted compounds to the selected target matched the affinity of the synthetic cholinesterase inhibitors Donepezil and Galantamine (−8.0 kcal/mol and 8.3 kcal/mol) respectively. The bioactive compounds exhibited significant affinity for the binding pockets of the selected target protein; indicating that these compounds may act as putative inhibitors of β-Site APP-cleaving enzyme (BACE 1) and are potential anti-Alzheimer drug candidates.
