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Issue 5, 2015
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Conformational preferences in the β-peptide oligomers of cis-2-amino-1-fluorocyclobutane-1-carboxylic acid

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Abstract

An efficient synthesis of cis-2-amino-1-fluorocyclobutane-1-carboxylic acid in single enantiomer form was established and protected homo-oligomers (2-, 4-, and 6-mers) of this cyclic cis-β-amino acid were prepared. Conformational analysis of these oligomers using IR, NMR and CD techniques in solution, supported by molecular modelling studies, suggested a strong conformational preference for a well-defined strand-like structure in which intra-residue hydrogen bonding is weak at best and is not consequential for adoption of the secondary structure. Single crystal X-ray analysis of the tetramer showed that a regular strand-like conformation is adopted in the solid state; only intermolecular hydrogen bonding networks are observed. The backbone topology and the 4-membered ring orientations are noticeably different from those of the tetramer of the corresponding non-fluorinated cis-β-amino acid.

Graphical abstract: Conformational preferences in the β-peptide oligomers of cis-2-amino-1-fluorocyclobutane-1-carboxylic acid

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Publication details

The article was received on 31 Oct 2014, accepted on 29 Nov 2014 and first published on 01 Dec 2014


Article type: Paper
DOI: 10.1039/C4NJ01929F
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Citation: New J. Chem., 2015,39, 3270-3279
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    Conformational preferences in the β-peptide oligomers of cis-2-amino-1-fluorocyclobutane-1-carboxylic acid

    A. Hassoun, C. M. Grison, R. Guillot, T. Boddaert and D. J. Aitken, New J. Chem., 2015, 39, 3270
    DOI: 10.1039/C4NJ01929F

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