Fluorinated Prolines as Conformational Tools and Reporters for Peptide and Protein Chemistry

Sanne J. M. Verhoork, Patrick M. Killoran, Christopher R. Coxon

Research output: Contribution to journalReview article

15 Citations (Scopus)
16 Downloads (Pure)

Abstract

Amide bonds at the proline nitrogen are particularly susceptible to rotation, affording cis and trans isomers. Installation of a stereochemically defined electron-withdrawing fluorine atom or fluorinated groups has the power to influence the cis-trans conformational preferences of the amide bond in X-(F)Pro (where X = any other amino acid). Advantageously, this also provides a sensitive reporter for 19F nuclear magnetic resonance (NMR) studies of protein conformation, interactions, and dynamics. We deliberately use the term "fluorinated prolines" as an all-encompassing term to describe proline analogues containing one or more fluorine atoms and to avoid confusion with the more well-known 4-fluoroprolines. This review presents a critical discussion of the growing repertoire of fluorinated prolines that have been described and, importantly, provides a comparison of their uses and relative influence on amide-bond conformation and discusses the significant potential of using 19F NMR as a tool to probe conformational changes in polypeptides.

Original languageEnglish
Pages (from-to)6132-6143
Number of pages12
JournalBiochemistry
Volume57
Issue number43
Early online date2 Oct 2018
DOIs
Publication statusPublished - 30 Oct 2018

ASJC Scopus subject areas

  • Biochemistry

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