IN SILICO IDENTIFICATION OF LIMODISSIMINAFROMKAWISTA (Limonia acidissima L.) AS APOTENTIALANGIOTENSIN-CONVERTING ENZYMEINHIBITORTHROUGH BIOAVAILABILITY PREDICTION, MOLECULARDOCKING, AND DYNAMICS SIMULATION
TL;DR
Findings suggest that limodissimin A is a promising candidate for ACE inhibition and further experimental validation is required to confirm its potential as a natural antihypertensive agent.
Abstract
Kawista (Limonia acidissima) is a plant known for its potential pharmacological properties, includingantihypertensive activity. This study aimed to evaluate the inhibitory potential of kawista secondary metabolitesagainst angiotensin-converting enzyme (ACE) using an in silico approach. A total of 31 compounds were identifiedand screened for oral bioavailability using the BOILED-Egg model, resulting in 20 compounds with favourablepharmacokinetic properties. Molecular docking analysis revealed that limodissimin A (mol 17) exhibitedthestrongest binding affinity toward ACE (−9.09 kcal/mol; Ki = 215.73 nM), with key interactions involving Lys511, His353, and His513. Molecular dynamics simulations further confirmed the stability of the ACE–ligand complex, asindicated by lower RMSD, reduced structural fluctuations, and decreased solvent exposure compared to the apoprotein. These findings suggest that limodissimin A is a promising candidate for ACE inhibition. Further experimental validation is required to confirm its potential as a natural antihypertensive agent.