Biochemistry (Moscow)

, Volume 81, Issue 4, pp 392–400 | Cite as

Interaction of chloramphenicol tripeptide analogs with ribosomes

  • A. G. Tereshchenkov
  • A. V. Shishkina
  • V. N. Tashlitsky
  • G. A. Korshunova
  • A. A. Bogdanov
  • N. V. SumbatyanEmail author


Chloramphenicol amine peptide derivatives containing tripeptide fragments of regulatory “stop peptides”–MRL, IRA, IWP–were synthesized. The ability of the compounds to form ribosomal complexes was studied by displacement of the fluorescent erythromycin analog from its complex with E. coli ribosomes. It was found that peptide chloramphenicol analogs are able to bind to bacterial ribosomes. The dissociation constants were 4.3-10 μM, which is 100-fold lower than the corresponding values for chloramphenicol amine–ribosome complex. Interaction of the chloramphenicol peptide analogs with ribosomes was simulated by molecular docking, and the most probable contacts of “stop peptide” motifs with the elements of nascent peptide exit tunnel were identified.


ribosome “stop peptides” chloramphenicol peptide derivatives nascent peptide exit tunnel 







(4,4-difluoro-4-bora-5,7-dimethyl)-3a,4a-diaza-s-indacene-3-pentanoic acid












liquid chromatography-mass spectrometry


peptide-nucleic acids


peptidyl transferase center


ribosomal tunnel


trifluoroacetic acid


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Supplementary material

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Copyright information

© Pleiades Publishing, Ltd. 2016

Authors and Affiliations

  • A. G. Tereshchenkov
    • 1
  • A. V. Shishkina
    • 2
  • V. N. Tashlitsky
    • 1
  • G. A. Korshunova
    • 2
  • A. A. Bogdanov
    • 1
    • 2
  • N. V. Sumbatyan
    • 1
    Email author
  1. 1.Faculty of ChemistryLomonosov Moscow State UniversityMoscowRussia
  2. 2.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia

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