integrating molecular docking and molecular dynamics simulation approaches for investigation of the affinity and interactions of berberine with class c β-lactamase

Background: antibiotic resistance is a significant health concern, as bacteria produce enzymes that inhibit antimicrobial drug activity, increasing disease generation. this study investigates the inhibitory effect of berberine on β-lactamase enzyme activity and antibiotic effectiveness. methods: molecular docking was utilized to find the binding pose and binding affinity of a new inhibitory ligand with the ampc enzyme using autodock software version 4.2.2. md simulations were performed in free form and complicated to understand the stability of the protein-ligand docked complex.results: the molecular docking result indicated the proper interaction between berberine and the ampc β-lactamase enzyme with a suitable binding pose and binding energy of -6.55 kcal/mol. the md simulation of systems verifies the docking result, which shows stable hydrogen bonds of berberine with ampc and good equivalence between rmsd, rmsf, sasa, etc.conclusion: this paper reveals that berberine, which is a natural ingredient with multiple medicinal characteristics, can be applied as a potential inhibitor of class c β-lactamase ampc. hence, the outcome of the calculations performed provides valuable data to design new inhibitors with therapeutic potential in order to control the β-lactamase activity.