Abstract
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.
Highlights
Hypertension or high blood pressure is one of the most top prevalent diseases in the world (Sorlie et al, 2014)
The docking of native ligand gave Root Mean Square Deviation (RMSD) value of 0.96Á (
We have conducted in silico molecular docking to study the potential of polyphenol compounds from P. pellucida as an angiotensin-converting enzyme (ACE) inhibitor
Summary
Hypertension or high blood pressure is one of the most top prevalent diseases in the world (Sorlie et al, 2014). One of the primary therapeutic agents for the treatment of hypertension is angiotensin-converting enzyme (ACE) inhibitors. ACE is one component of the renin-angiotensin-aldosterone system and plays a crucial role in the regulation of blood pressure (Skeggs et al, 1953; 1957). ACE has two isoforms, Ahmad et al / Journal of Applied Pharmaceutical Science 9 (08); 2019: 025-031 including: (1) glycoprotein form in somatic tissue with single large polypeptide chain of 1,277 amino acid and (2) in germinal cells that are synthesized in the form of lower molecular mass and play a role in sperm maturation and sperm binding of oviduct epithelium (Natesh et al, 2003; 2004). The crystal structure data from ACE is available in the form of PDB files that can be used for in silico molecular docking study
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