Interaction of chloramphenicol tripeptide analogs with ribosomes View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-04

AUTHORS

A. G. Tereshchenkov, A. V. Shishkina, V. N. Tashlitsky, G. A. Korshunova, A. A. Bogdanov, N. V. Sumbatyan

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. More... »

PAGES

392-400

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s000629791604009x

DOI

http://dx.doi.org/10.1134/s000629791604009x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1039415269

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27293096


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