Interaction of chloramphenicol tripeptide analogs with ribosomes
- Authors: Tereshchenkov A.G.1, Shishkina A.V.2, Tashlitsky V.N.1, Korshunova G.A.2, Bogdanov A.A.1,2, Sumbatyan N.V.1
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Affiliations:
- Faculty of Chemistry
- Belozersky Institute of Physico-Chemical Biology
- Issue: Vol 81, No 4 (2016)
- Pages: 392-400
- Section: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150836
- DOI: https://doi.org/10.1134/S000629791604009X
- ID: 150836
Cite item
Abstract
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.
About the authors
A. G. Tereshchenkov
Faculty of Chemistry
Email: sumbtyan@belozersky.msu.ru
Russian Federation, Moscow, 119991
A. V. Shishkina
Belozersky Institute of Physico-Chemical Biology
Email: sumbtyan@belozersky.msu.ru
Russian Federation, Moscow, 119991
V. N. Tashlitsky
Faculty of Chemistry
Email: sumbtyan@belozersky.msu.ru
Russian Federation, Moscow, 119991
G. A. Korshunova
Belozersky Institute of Physico-Chemical Biology
Email: sumbtyan@belozersky.msu.ru
Russian Federation, Moscow, 119991
A. A. Bogdanov
Faculty of Chemistry; Belozersky Institute of Physico-Chemical Biology
Email: sumbtyan@belozersky.msu.ru
Russian Federation, Moscow, 119991; Moscow, 119991
N. V. Sumbatyan
Faculty of Chemistry
Author for correspondence.
Email: sumbtyan@belozersky.msu.ru
Russian Federation, Moscow, 119991