Binding and Action of Amino Acid Analogs of Chloramphenicol upon the Bacterial Ribosome.

ABSTRACT: Antibiotic chloramphenicol (CHL) binds with a moderate affinity at the peptidyl transferase center of the bacterial ribosome and inhibits peptide bond formation. As an approach for modifying and potentially improving properties of this inhibitor, we explored ribosome binding and inhibitory activity of a number of amino acid analogs of CHL. The L-histidyl analog binds to the ribosome with the affinity exceeding that of CHL by 10 fold. Several of the newly synthesized analogs were able to inhibit protein synthesis and exhibited the mode of action that was distinct from the action of CHL. However, the inhibitory properties of the semi-synthetic CHL analogs did not correlate with their affinity and in general, the amino acid analogs of CHL were less active inhibitors of translation in comparis

SUBMITTER: Tereshchenkov AG 

PROVIDER: S-EPMC6023675 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature