Open AccessPotential of MurA Enzyme and GBAP in Fsr Quorum Sensing System as Antibacterial Drugs Target: In vitro and In silico Study of Antibacterial Compounds from Myrmecodia pendans
Author(s) -
Eti Apriyanti,
Mieke Hemiawati Satari,
Dikdik Kurnia
Publication year - 2021
Publication title -
combinatorial chemistry and high throughput screening
Language(s) - English
Resource type - Journals
eISSN - 1875-5402
pISSN - 1386-2073
DOI - 10.2174/1386207323666200628111348
Subject(s) - mura , serine protease , taxifolin , in silico , quorum sensing , chemistry , biochemistry , protease , antibacterial activity , docking (animal) , serine , stereochemistry , enzyme , quercetin , bacteria , biology , antioxidant , medicine , genetics , nursing , liquid crystal display , virulence , computer science , gene , operating system
Background: Increasing the resistance issue has become the reason for the developmentof new antibacterial in crucial condition. Many ways are tracked to determine the most effectiveantibacterial agent. Some proteins that are a key role in bacteria metabolism are targeted, includingMurA in cell wall biosynthesis and gelatinase biosynthesis-activating pheromone (GBAP) in FsrQuorum Sensing (QS) system. Objective: The objective of this research is the analysis of compounds 1-4 from M. pendans asantibacterial and anti-QS activity trough protein inhibition by in silico study; focus on thestructure-activity relationships, to appraise their role as an antibacterial and anti-QS agent in themolecular level. Methods: Both activities of M. pendans compounds (1-4) were analyzed by in silico, compared toFosfomycin, Ambuic acid, Quercetin, and Taxifolin as a standard. Chemical structures of M.pendans compounds were converted using an online program molview. The compounds weredocked to MurA, GBAP, gelatinase and serine protease using Autodock Vina in Pyrx 0.8 followedPYMOL to visualization and proteis.plus program to analyze of the complex. Results: All compounds from M. pendans bound on MurA, GBAP, gelatinase and serine proteaseexcept compound 2. This biflavonoid did not attach to MurA and serine protease yet is thefavorable ligand for GBAP and gelatinase with the binding affinity of -6.9 and -9.4 Kcal/molrespectively. Meanwhile, for MurA and serine protease, compound 4 is the highest of bondingenergy with values of -8.7 and -6.4 Kcal/mol before quercetin (MurA, -8.9 Kcal/mol) and taxifolin(serine protease, -6.6 Kcal/mol). Conclusion: Based on the data, biflavonoid acts better as anti-QS than an inhibitor of MurAenzyme while the others can be acted into both of them either the therapeutic agent of anti-QS orantibacterial agent of MurA inhibitor.