Investigating Structural Changes in Chloramphenicol-۲۳S rRNA Interactions: AMolecular Docking Study of Mutations in E. coli Ribosome

Chloramphenicol, a potent antibiotic, disrupts protein synthesis in prokaryotes by targeting the ۵۰Ssubunit of bacterial ribosomes. In this study, we investigate the impact of mutations within the peptidyltransferase loop of the ۲۳S rRNA on chloramphenicol binding using in silico molecular dockinganalysis. Specifically, G۲۵۰۵A, A۲۰۵۷G, A۲۰۵۸G, and G۲۰۶۱A mutations in the ۲۳S rRNA wereexamined. Molecular docking simulations were conducted using AutoDock Vina software, revealingsignificant structural alterations in chloramphenicol-۲۳S rRNA interactions between wild and mutanttypes. Analysis of binding affinity scores, hydrogen bonding patterns, and hydrophobic interactionselucidates how mutations influence chloramphenicol binding and potentially contribute to antibioticresistance in E. coli. The G۲۵۰۵A and A۲۰۵۷G mutations show a slight reduction in binding affinity,potentially contributing to moderate resistance, while mutations A۲۰۵۸G and G۲۰۶۱A maintain bindingaffinities similar to the wild type. Our findings shed light on the molecular mechanisms underlyingchloramphenicol resistance, offering insights for developing novel therapeutic strategies againstantibiotic-resistant bacteria.

کلیدواژه ها:

Molecular docking ، Peptidyl transferase loop ، ۲۳S rRNA ، Chloramphenicol ، Escherichiacoli