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

Sara C. McFarlan, Robert Vince

Research output: Contribution to journalArticlepeer-review

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

Bibliographical note

Funding Information:
We thank Jay Br ownell for assistance in the biological assays. This investigation was supported by Grants CA 13592 and CA 23263 from the National Cancer Institute, Department of Health, Education, and Welfare.

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