integrating molecular docking and molecular dynamics simulation approaches for investigation of the affinity and interactions of quercetin with class d betalactamase, oxa-10

Introduction: the misuse of β-lactam antibiotics has led to the development of β-lactamase-producing organisms, which inhibit β-lactam activity by hydrolyzing the peptide bond. this study aims to investigate the inhibitory effect of quercetin, a natural composite and isoquinoline alkaloid, on β-lactamase enzyme action, potentially increasing antibiotic effectiveness. materials and methods: this study utilized computational techniques like molecular docking and md simulation to predict the binding mode and possible conformation poses of quercetin with the oxa-10 β-lactamase enzyme. autodock software was used for docking, while gromacs 2019.6 package was used for md simulations to study molecular complex behavior over time.results: the outcomes of the molecular docking analysis revealed a favorable interaction between quercetin and the oxa-10 β-lactamase enzyme, as evidenced by a binding energy of -5.95 kcal/mol and a suitable binding mode. md simulations confirmed the docking results, showing stable hydrogen bonds between quercetin and oxa-10, as well as comparable rmsd, rmsf, sasa values, and other parameters.discussion: this research shows the potential of quercetin, a natural compound with multiple medicinal effects, as a possible inhibitor of the class d type β-lactamase oxa-10. therefore, this study maintains valuable intuition for designing new inhibitors of antimicrobial resistance to combat β-lactamase activity.