Molecular Docking, Physicochemical and Drug-likeness Properties of Isolated Compounds from Garcinia latissima Miq. on Elastase Enzyme: In Silico Analysis

Abstract

Garcinia latissima Miq. belongs to the Clusiaceae family that has been studied with activity as an antibacterial and anti-elastase in vitro. The inhibitory ability of the elastase enzyme from the G. latissima extract. This needs to be tested further by an in silico molecular docking study of the compound. Previous studies have shown that 4-oxo-β-lactam crystals are selective against the human neutrophil elastase (an enzyme protease). It has a structural relationship with its activity to become the basis for inhibiting the elastase enzyme. The purpose of this in silico study was to test whether the isolated compounds from G. latissima (including friedelin, 6-deoxyjacareubin, amentoflavone, and Robusta flavone). The in silico molecular docking method used was Autodock 4.2.6 molecular docking software. This protocol is used to test friedelin, 6-deoxyjacareubin, amentoflavone, and Robusta flavone as ligands for the elastase enzyme receptor. The protocol's output was analyzed using the Accelrys Discovery Studio Visualizer 4.0 post-docking analysis method. The results showed that isolated compounds, including amentoflavone, friedelin, and 6-deoxyjacareubin, are active ligands against porcine pancreatic elastase with the free binding energy of -10.94, -7.17, and -6.72 kcal/mol, respectively, and form hydrogen bonds, van der Walls, alkyl, electrostatic, and hydrophobic interaction. In silico physicochemical, lipophilicity, water-soluble, pharmacokinetics, and drug-likeness properties prediction showed characteristics prediction of isolated compound. This study provides an overview of the molecular interactions of isolates compounds from G. latissima against the elastase enzyme. Key words: Drug likeness, Garcinia latissima Miq., Molecular docking study, Elastase enzyme, Physicochemical properties.