چکیده
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Chloramphenicol, a potent antibiotic, disrupts protein synthesis in prokaryotes by targeting the 50S subunit of bacterial ribosomes. In this study, we investigate the impact of mutations within the peptidyl transferase loop of the 23S rRNA on chloramphenicol binding using in silico molecular docking analysis. Specifically, G2505A, A2057G, A2058G, and G2061A mutations in the 23S rRNA were examined. Molecular docking simulations were conducted using AutoDock Vina software, revealing significant structural alterations in chloramphenicol-23S rRNA interactions between wild and mutant types. Analysis of binding affinity scores, hydrogen bonding patterns, and hydrophobic interactions elucidates how mutations influence chloramphenicol binding and potentially contribute to antibiotic resistance in E. coli. The G2505A and A2057G mutations show a slight reduction in binding affinity, potentially contributing to moderate resistance, while mutations A2058G and G2061A maintain binding affinities similar to the wild type. Our findings shed light on the molecular mechanisms underlying chloramphenicol resistance, offering insights for developing novel therapeutic strategies against antibiotic-resistant bacteria.
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