Interaction of chloramphenicol tripeptide analogs with ribosomes
- Autores: Tereshchenkov A.1, Shishkina A.2, Tashlitsky V.1, Korshunova G.2, Bogdanov A.1,2, Sumbatyan N.1
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Afiliações:
- Faculty of Chemistry
- Belozersky Institute of Physico-Chemical Biology
- Edição: Volume 81, Nº 4 (2016)
- Páginas: 392-400
- Seção: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150836
- DOI: https://doi.org/10.1134/S000629791604009X
- ID: 150836
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Resumo
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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Sobre autores
A. Tereshchenkov
Faculty of Chemistry
Email: sumbtyan@belozersky.msu.ru
Rússia, Moscow, 119991
A. Shishkina
Belozersky Institute of Physico-Chemical Biology
Email: sumbtyan@belozersky.msu.ru
Rússia, Moscow, 119991
V. Tashlitsky
Faculty of Chemistry
Email: sumbtyan@belozersky.msu.ru
Rússia, Moscow, 119991
G. Korshunova
Belozersky Institute of Physico-Chemical Biology
Email: sumbtyan@belozersky.msu.ru
Rússia, Moscow, 119991
A. Bogdanov
Faculty of Chemistry; Belozersky Institute of Physico-Chemical Biology
Email: sumbtyan@belozersky.msu.ru
Rússia, Moscow, 119991; Moscow, 119991
N. Sumbatyan
Faculty of Chemistry
Autor responsável pela correspondência
Email: sumbtyan@belozersky.msu.ru
Rússia, Moscow, 119991