The utilization of medicinal plants has long been explored for the discovery of antibacterial agents and the most effective mechanisms or new targets that can prevent and control the spread of antibiotic resistance. One kind of bacterial cell wall inhibition is the inactivation of the MurA enzyme that contributes to the formation of peptidoglycan. Another approach is to interfere with the cell–cell communication of bacteria called the Quorum sensing (QS) system. The blocking of auto-inducer such as gelatinase biosynthesis-activating pheromone (GBAP) can also suppress the virulence factors of gelatinase and serine protease. This research, in particular, aims to analyze lead compounds as antibacterial and anti-QS agents from Gambir (Uncaria gambir Roxburgh) through protein inhibition by in silico study. Antibacterial agents were isolated by bioactivity-guided isolation using a combination of chromatographic methods, and their chemical structures were determined by spectroscopic analysis methods. The in vitro antibacterial activity was evaluated by disc diffusion methods to determine inhibitory values. Meanwhile, in the in silico analysis, the compound of Uncaria gambir was used as ligand and compared with fosfomycin, ambuic acid, quercetin, and taxifolin as the standard ligand. These ligands were attached to MurA, GBAP, gelatinase, and serine proteases using Autodock Vina in PyRx 0.8 followed by PYMOL for combining the ligand conformation and proteins. plus programs to explore the complex, and visualized by Discovery Studio 2020 Client program. The antibacterial agent was identified as catechin that showed inhibitory activity against Enterococcus faecalis ATCC 29212 with inhibition zones of 11.70 mm at 10%, together with MIC and MBC values of 0.63 and 1.25 μg/mL, respectively. In the in silico study, the molecular interaction of catechin with MurA, GBAP, and gelatinase proteins showed good binding energy compared with two positive controls, namely fosfomycin and ambuic acid. It is better to use catechin–MurA (−8.5 Kcal/mol) and catechin–gelatinase (−7.8 Kcal/mol), as they have binding energies which are not marginally different from quercetin and taxifolin. On the other hand, the binding energy of serine protease is lower than quercetin, taxifolin, and ambuic acid. Based on the data, catechin has potency as an antibacterial through the inhibition of GBAP proteins, gelatinase, and serine protease that play a role in the QS system. This is the first discovery of the potential of catechin as an alternative antibacterial agent with an effective mechanism to prevent and control oral disease affected by antibiotic resistance.
Background: Ant-nest (Myrmecodia pendans) is an epiphytic plant that can prevent several diseases, including bacterial infections. Diarrhea is caused by Escherichia coli bacteria, while infections in the oral cavity can be caused by Enterococcus faecalis bacteria. Antibacterial activity is also influenced by conditions of Reactive Oxygen Species (ROS). Antioxidants are needed to inhibit the formation of excess ROS in the body. Superoxide anion radicals are included in the generation of ROS, which are produced by several enzymes, such as nicotinamide-adenine dinucleotide phosphate (NADPH) oxidase or commonly known as Nox and xanthine oxidase (XO). Background: Ant-nest (Myrmecodia pendans) is an epiphytic plant that can prevent several diseases, including bacterial infections. Diarrhea is caused by Escherichia coli bacteria, while infections in the oral cavity can be caused by Enterococcus faecalis bacteria. Antibacterial activity is also influenced by conditions of Reactive Oxygen Species (ROS). Antioxidants are needed to inhibit the formation of excess ROS in the body. Superoxide anion radicals are included in the generation of ROS, which are produced by several enzymes, such as nicotinamide-adenine dinucleotide phosphate (NADPH) oxidase or commonly known as Nox and xanthine oxidase (XO). Objective: This study aimed to determine the potential of M. pendans as an antibacterial in vitro and in silico correlation in the formation of superoxide anion radicals. objective: To determine the potential of M. pendans as an antibacterial in vitro and in silico correlation in the formation of superoxide anion radicals. Methods and Materials: The compounds were obtained by column chromatography method, followed by a spectroscopic examination. In vitro test using the disc diffusion method and in silico test using AutoDock 4.2 program were conducted with positive control fosfomycin and allopurinol, tethered to MurA, Nox, and XO enzymes, and visualized using the Discovery Studio 2020. Results: Compound 1 (oleanolic acid ) and compound 2 (pomolic acid) demonstrated antibacterial activity against E.coli but no activity against E. faecalis. Compound 3 (acid-3-hydroxy-eupan-20,24-dien-26-oic) demonstrated no activity against these two bacteria. Based on the in silico results, compound 3 had the best binding energy affinity for all MurA, Nox, and XO enzymes of -6.89, -9.35, and -9.75 Kcal/mol, respectively. Similarly, compounds 1 and 2 had good binding energies for Nox protein of -9.29 Kcal/mol and -6.54 Kcal/mol and XO of -7.66 and -4.7 Kcal/mol, respectively. Conclusion: In vitro results against E.coli and E. faecalis bacteria showed inhibition by compounds 1 and 2 but not by compound 3. Meanwhile, in in silico analysis, all the compounds showed potential as an inhibitor of superoxide anion radicals generated by enzymes Nox and XO. conclusion: In vitro results against E.coli and E. faecalis bacteria showed inhibition by compounds 1 and 2, but not by compound 3. Meanwhile, based on the results of in silico data, compounds 1-3 had the potential to inhibit superoxide radicals. anions to the enzymes Nox and XO. other: -
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.