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Issue 11, 2015
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γ-(S)-Trifluoromethyl proline: evaluation as a structural substitute of proline for solid state 19F-NMR peptide studies

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Abstract

γ-(4S)-Trifluoromethyl proline was synthesised according to a modified literature protocol with improved yield on a multigram scale. Conformational properties of the amide bond formed by the amino acid were characterised using N-acetyl methyl ester model. The amide populations (s-trans vs. s-cis) and thermodynamic parameters of the isomerization were found to be similar to the corresponding values for intact proline. Therefore, the γ-trifluoromethyl proline was suggested as a structurally low-disturbing proline substitution in peptides for their structural studies by 19F-NMR. Indeed, the exchange of native proline for γ-trifluoromethyl proline in the peptide antibiotic gramicidin S was shown to preserve the overall amphipathic peptide structure. The utility of the amino acid as a selective 19F-NMR label was demonstrated by observing the re-alignment of the labelled gramicidin S in oriented lipid bilayers.

Graphical abstract: γ-(S)-Trifluoromethyl proline: evaluation as a structural substitute of proline for solid state 19F-NMR peptide studies

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Publication details

The article was received on 07 Jan 2015, accepted on 13 Feb 2015 and first published on 13 Feb 2015


Article type: Paper
DOI: 10.1039/C5OB00034C
Citation: Org. Biomol. Chem., 2015,13, 3171-3181
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    γ-(S)-Trifluoromethyl proline: evaluation as a structural substitute of proline for solid state 19F-NMR peptide studies

    V. Kubyshkin, S. Afonin, S. Kara, N. Budisa, P. K. Mykhailiuk and A. S. Ulrich, Org. Biomol. Chem., 2015, 13, 3171
    DOI: 10.1039/C5OB00034C

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