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

Verhoork, SJM, Killoran, PM and Coxon, CR (2018) Fluorinated Prolines as Conformational Tools and Reporters for Peptide and Protein Chemistry. Biochemistry, 57 (43). pp. 6132-6143. ISSN 1520-4995

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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.

Item Type: Article
Uncontrolled Keywords: 0601 Biochemistry and Cell Biology, 1101 Medical Biochemistry and Metabolomics, 0304 Medicinal and Biomolecular Chemistry
Subjects: Q Science > QD Chemistry
R Medicine > RM Therapeutics. Pharmacology
Divisions: Pharmacy & Biomolecular Sciences
Publisher: American Chemical Society
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Date Deposited: 16 Jan 2019 12:52
Last Modified: 17 Jan 2019 21:31
DOI or Identification number: 10.1021/acs.biochem.8b00787
URI: http://researchonline.ljmu.ac.uk/id/eprint/9950

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