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

Sergio Celis, Esther Gorrea, Pau Nolis, Ona Illa, Rosa M. Ortuño

Research output: Contribution to journalArticleResearchpeer-review

21 Citations (Scopus)

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 C 2 or C 4 linear segment to a helical folding for those with a C 3 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. © 2012 The Royal Society of Chemistry.
Original languageEnglish
Pages (from-to)861-868
JournalOrganic and Biomolecular Chemistry
Volume10
Issue number4
DOIs
Publication statusPublished - 28 Jan 2012

Fingerprint

Dive into the research topics of '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'. Together they form a unique fingerprint.

Cite this