What is one of the primary functions of chloramphenicol in bacterial cells?

Chloramphenicol is an antibiotic that primarily works by blocking peptide bond formation during protein synthesis in bacterial cells. It achieves this by binding to the 50S subunit of the bacterial ribosome, which is essential for translating mRNA into proteins. By inhibiting the activity of the ribosome, chloramphenicol prevents the incorporation of amino acids into growing polypeptide chains, effectively halting protein production. This mechanism is particularly effective against a wide range of bacteria, making chloramphenicol a valuable antibiotic in treating various bacterial infections.

Other functions listed, such as inhibiting cell wall synthesis, disrupting membrane integrity, and preventing DNA replication, are associated with different antibiotics or mechanisms of action. For example, antibiotics that inhibit cell wall synthesis include penicillins, while those that disrupt membrane integrity include polymyxins. By understanding chloramphenicol’s specific mechanism of blocking peptide bond formation, one can appreciate its role in combating bacterial infections and the reason behind its usage in clinical settings.