Potential Role of Betel Leaf (Piper betle L.) Water Extract as Antibacterial Escherichia coli Through Inhibition of β-Ketoacyl-[Acyl Carrier Protein] Synthase I http://www.doi.org/10.26538/tjnpr/v6i11.10
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Abstract
The exploration of bioactive compounds from herbal plants as inhibitors of fatty acid synthesis without adverse side effects is still the focus of the discovery and development of antibacterial drugs, especially to fight infections in chronic wounds. This study aimed to investigate the biological function of the bioactive compound of Piper betle L. leaf extract in inhibiting the target protein of Escherichia coli. 3D structure of the bioactive compound and thiolactomycin (as a positive control) were downloaded from PubChem. The Protein Data Bank database was used to retrieve the 3D structure of β-Ketoacyl-[Acyl Carrier Protein] Synthase I (FabB). Prediction of the active site of FabB was predicted using the Molegro Virtual Docker 5.0 program. Molecular interactions of the compound and target protein were analyzed using Molegro virtual docking version 5, superimposed using PyMol version 2.2, and visualized using the Discovery Studio program version 21.1.1. The results showed that the five bioactive compounds of Piper betle L. (eugenol, catechin, caffeic acid, quercetin, and ascorbic acid) could bind to the active site of FabB. All compounds were found to bind to the residues ALA271, PRO272 and HIS298. The catechin-FabB complex showed the lowest binding energy. This finding indicates that the Piper betle L. leaf extract's bioactive compound may inhibit the target protein of E. coli β - Ketoacyl-[Acyl Carrier Protein] Synthase I (FabB), which leads to the
control of bacterial infection in chronic wounds at the cellular level.
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