The relevance of the relative configuration in the folding of hybrid peptides containing β-cyclobutane amino acids and γ-amino-L-proline residues

Ona Illa, José Antonio Olivares, Pau Nolis, Rosa M. Ortuño

Research output: Contribution to journalArticleResearchpeer-review

3 Citations (Scopus)

Abstract

© 2017 Elsevier Ltd Four new series of diastereomeric β,γ-di- and β,γ-tetrapeptides derived from conveniently protected (1R,2S)- and (1S,2S)-2-aminocyclobutane-1-carboxylic acid and cis- and trans-γ-amino-L-proline joined in alternation have been synthesized. High resolution NMR experiments show that peptides containing trans-cyclobutane amino acid residues adopt a more folded structure in solution than those containing a cis-cyclobutane residue, which adopt a strand-like structure. The cis/trans relative configuration of the cyclobutane residue is the origin of the folding pattern of each peptide due to either intra- or inter-residue hydrogen-bonded ring formation, whereas the cis/trans isomerism of the γ-amino-L-proline residue does not have a significantly relevant role on the folding ability of these peptides.
Original languageEnglish
Pages (from-to)6286-6295
JournalTetrahedron
Volume73
Issue number44
DOIs
Publication statusPublished - 2 Nov 2017

Keywords

  • Cyclobutane
  • Foldamers
  • Hybrid peptides
  • Hydrogen bonds
  • γ-Amino-L-proline

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