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Issue 4, 2012
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Designing hybrid foldamers: the effect on the peptide conformational bias of β- versus α- and γ-linear residues in alternation with (1R,2S)-2-aminocyclobutane-1-carboxylic acid

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Abstract

Several oligomers constructed with (1R,2S)-2-aminocyclobutane-1-carboxylic acid and glycine, β-alanine, and γ-amino butyric acid (GABA), respectively, joined in alternation have been synthesized and studied by means of NMR and CD experiments as well as with computational calculations. Results account for the spacer length effect on folding and show that conformational preference for these hybrid peptides can be tuned from β-sheet-like folding for those containing a C2 or C4 linear segment to a helical folding for those with a C3 spacer between cyclobutane residues. The introduction of cyclic spacers between these residues does not modify the extended ribbon-type structure previously manifested in poly(cis-cyclobutane) β-oligomers.

Graphical abstract: Designing hybrid foldamers: the effect on the peptide conformational bias of β- versus α- and γ-linear residues in alternation with (1R,2S)-2-aminocyclobutane-1-carboxylic acid

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Publication details

The article was received on 14 Sep 2011, accepted on 11 Oct 2011 and first published on 12 Oct 2011


Article type: Paper
DOI: 10.1039/C1OB06575K
Citation: Org. Biomol. Chem., 2012,10, 861-868
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    Designing hybrid foldamers: the effect on the peptide conformational bias of β- versus α- and γ-linear residues in alternation with (1R,2S)-2-aminocyclobutane-1-carboxylic acid

    S. Celis, E. Gorrea, P. Nolis, O. Illa and R. M. Ortuño, Org. Biomol. Chem., 2012, 10, 861
    DOI: 10.1039/C1OB06575K

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