Investigating Structural Changes in Chloramphenicol-23S rRNA Interactions: AMolecular Docking Study of Mutations in E. coli Ribosome

Chloramphenicol, a potent antibiotic, disrupts protein synthesis in prokaryotes by targeting the 50Ssubunit of bacterial ribosomes. In this study, we investigate the impact of mutations within the peptidyltransferase loop of the 23S rRNA on chloramphenicol binding using in silico molecular dockinganalysis. Specifically, G2505A, A2057G, A2058G, and G2061A mutations in the 23S rRNA wereexamined. Molecular docking simulations were conducted using AutoDock Vina software, revealingsignificant structural alterations in chloramphenicol-23S 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 G2505A and A2057G mutations show a slight reduction in binding affinity,potentially contributing to moderate resistance, while mutations A2058G and G2061A 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.

Investigating Structural Changes in Chloramphenicol-23S rRNA Interactions: AMolecular Docking Study of Mutations in E. coli Ribosome Keywords:

Molecular docking , Peptidyl transferase loop , 23S rRNA , Chloramphenicol , Escherichiacoli