Interaction of chloramphenicol tripeptide analogs with ribosomes
- 作者: Tereshchenkov A.1, Shishkina A.2, Tashlitsky V.1, Korshunova G.2, Bogdanov A.1,2, Sumbatyan N.1
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隶属关系:
- Faculty of Chemistry
- Belozersky Institute of Physico-Chemical Biology
- 期: 卷 81, 编号 4 (2016)
- 页面: 392-400
- 栏目: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150836
- DOI: https://doi.org/10.1134/S000629791604009X
- ID: 150836
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详细
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.
作者简介
A. Tereshchenkov
Faculty of Chemistry
Email: sumbtyan@belozersky.msu.ru
俄罗斯联邦, Moscow, 119991
A. Shishkina
Belozersky Institute of Physico-Chemical Biology
Email: sumbtyan@belozersky.msu.ru
俄罗斯联邦, Moscow, 119991
V. Tashlitsky
Faculty of Chemistry
Email: sumbtyan@belozersky.msu.ru
俄罗斯联邦, Moscow, 119991
G. Korshunova
Belozersky Institute of Physico-Chemical Biology
Email: sumbtyan@belozersky.msu.ru
俄罗斯联邦, Moscow, 119991
A. Bogdanov
Faculty of Chemistry; Belozersky Institute of Physico-Chemical Biology
Email: sumbtyan@belozersky.msu.ru
俄罗斯联邦, Moscow, 119991; Moscow, 119991
N. Sumbatyan
Faculty of Chemistry
编辑信件的主要联系方式.
Email: sumbtyan@belozersky.msu.ru
俄罗斯联邦, Moscow, 119991
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