Chloramphenicol overlaps with the binding site of the A-site (t-RNA) & 23s rRNA, to prevent peptide bond formation. In 23s rRNA of the ribosome chloramphenicol binds to A2451 & A2452 residues and inhibits Peptide bond formation.

Antibiotic inhibiting peptide bond formation

Peptide bonds are essential for the formation of proteins in bacteria. Inhibition of peptide bond formation can lead to the inability of bacteria to synthesize proteins, leading to bacterial cell death. One antibiotic that inhibits peptide bond formation is Chloramphenicol.

Explanation

Chloramphenicol is a broad-spectrum antibiotic that inhibits the activity of the bacterial ribosome. It binds to the 50S subunit of the bacterial ribosome and prevents the formation of peptide bonds between the amino acids carried by the transfer RNA molecules. This results in the inhibition of protein synthesis in bacteria, leading to bacterial cell death.

Chloramphenicol is effective against a wide range of bacteria, including Gram-positive and Gram-negative bacteria. However, its use is limited due to its potential toxicity. It can cause serious side effects such as bone marrow suppression, which can lead to anemia, leukopenia, and thrombocytopenia.

Conclusion

Chloramphenicol is an antibiotic that inhibits peptide bond formation in bacteria, leading to the inhibition of protein synthesis and bacterial cell death. Its broad-spectrum activity makes it effective against a wide range of bacteria. However, its use is limited due to its potential toxicity.