Angiotensin-converting enzyme inhibitory activity of polyphenolic compounds from Peperomia pellucida (L) Kunth: An in silico molecular docking study

This study aimed to predict the potential activity and interaction conformation of polyphenolic compounds from Peperomia pellucida (L) Kunth (nine compounds) with angiotensin-converting enzyme (ACE) macromolecule by in silico molecular docking study. The crystal structure of ACE as a molecular target was obtained from the PDB database (PDB ID: 1UZF) with captopril as a native ligand. Molecular docking analysis was performed using AutoDockZn (100 docking runs) based on the active site of Zn2+, the central grid was placed on Zn2+ with a box size of 40A × 40A × 40A and a center of 40.835A × 34.382A × 44.607A for selective inhibitors (MCO702) with a spacing of 0.375A. Based on the docking results demonstrated that the prediction of each polyphenol compounds from P. pellucida has the potential of active as ACE inhibitors, it was indicated that docking results of each compound has lower affinity compared to captopril (with binding affinity of −6.36 kcal/mol and the inhibition constant 21.81 μM), where the most moderate binding affinity (the most potential) was tetrahydrofuran lignin ((1R,2S,3S,5R)-3,5-bis(4-hydroxy- 3,5-dimethoxyphenyl)cyclopentane-1,2-diyl)bis-(methylene) diacetate) of −8.66 kcal/mol and the highest binding affinity (the less potential) was dillapiole (6-allyl-4,5-dimethoxybenzo[d][1,3]dioxole) of −4.99 kcal/mol, although with different forms of interaction, bond, and constant inhibition. Based on the interaction of ACE binding site, 5,6,7-trimethoxy-4-(2,4,5-trimethoxyphenyl)-3,4-dihydronaphthalen-1(2H)-one showed the most similar interaction with the captopril ligand. These results are preliminary data for further research with predictions of target compound biological activity and interaction quickly, accurately, and inexpensively. Keywords: Angiotensin-converting enzyme, binding affinity, molecular docking, Peperomia pellucida (L) Kunth, polyphenolics.