Molecular docking analysis of natural compounds as Human neutrophil elastase (HNE) inhibitors

In recent years regulation of the enzymatic activity of human neutrophil elastase (HNE) has been the main focus of investigation, due to its potential therapeutic application in medicinal field. In the present study, the docking behaviour of human neutrophil elastase (HNE) with 14 different ligands namely Chrotacumines-A, B, C, GrandolsB, D, G, Rohitukine, Quercitin, Ellagic acid, Artoindonesianin-F, Origanol-A Thymoquinone, Embelin and Vilangin was evaluated along with their putative binding sites using Discovery Studio Version 3.1. In addition, molecular descriptors analysis using Molinspiration online tool was also carried out. The molecular physicochemical analysis revealed that Quercitin, Artoindonesianin-F & Origanol-A violated the five rules of thumb. With regard to druglikeness property, Thymoquinone exhibited better score compared to all other ligands. Docking studies and binding free energy calculations revealed that Vilangin has maximum interaction energy (-50.1 kcal/mol) and Thymoquinone with the least interaction energy (-18.1 kcal/mol) as compared to the other investigated ligands. Quercitrin is the only ligand showed interaction with Ser 195 amino acid residue. Therefore, it is strongly suggested that the present study outcomes might provide new insight in understanding these 14 ligands, as potential candidates for human neutrophil elastase (HNE) inhibitory activity.