Jump to main content
Jump to site search

Issue 4, 2012
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation

Supplementary files

Article information


Submitted
14 Sep 2011
Accepted
11 Oct 2011
First published
12 Oct 2011

Org. Biomol. Chem., 2012,10, 861-868
Article type
Paper

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

Social activity

Search articles by author

Spotlight

Advertisements