Inhibition of peptidyltransferase and possible mode of action of a dipeptidyl chloramphenicol analog

Sara C. McFarlan, Robert Vince

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

A dipeptidyl chloramphenicol analog, D-threo-2-(L-phenylalanylglycyl)amino-3-p-nitrophenyl-1,3-propanediol, has been prepared and examined as an inhibitor of ribosomal peptidyltransferase. The analog is a more effective inhibitor of poly (U,C) directed protein biosynthesis in an Escherichia coli cell-free system than chloramphenicol and shows inhibitory activity equal to the parent antibiotic in the transpeptidation reaction. These results and the common structural features of puromycin and this compound suggest a model for the binding modes of chloramphenicol and chloramphenicol analogs. This proposal invokes four major binding pockets at the A-site of the peptidyltransferase center.

Original languageEnglish (US)
Pages (from-to)748-754
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume122
Issue number2
DOIs
StatePublished - Jul 31 1984

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