Interaction of Chloramphenicol Tripeptide Analogs with Ribosomes

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A. G. Tereshchenkov¹, A. V. Shishkina², V. N. Tashlitsky¹, G. A. Korshunova², A. A. Bogdanov^1,2, and N. V. Sumbatyan^1*

¹Lomonosov Moscow State University, Faculty of Chemistry, 119991 Moscow, Russia; E-mail: sumbtyan@belozersky.msu.ru

²Lomonosov Moscow State University, Belozersky Institute of Physico-Chemical Biology, 119991 Moscow, Russia

^* To whom correspondence should be addressed.

Received September 24, 2015; Revision received November 18, 2015

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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.

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KEY WORDS: ribosome, “stop peptides”, chloramphenicol, peptide derivatives, nascent peptide exit tunnel

DOI: 10.1134/S000629791604009X

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