The fourth helical secondary structure of β-peptides: The (P)-28-helix of a β-hexapeptide consisting of (2R,3S)-3-amino-2-hydroxy acid residues

Karl Gademann, Andreas Häne, Magnus Rueping, Bernhard Jaun, Dieter Seebach*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

82 Scopus citations

Abstract

Small change with great effect! An oligomer of α-hydroxy-β-amino acids folds into a right-handed helical structure (see picture) in MeOH; in contrast, the methyl analogue has a pleated sheet structure. Including this new helix, four different helical secondary structures of β-peptides have been discovered - a structural diversity that should allow the generation of elaborate proteomimetics.

Original languageEnglish (US)
Pages (from-to)1534-1537
Number of pages4
JournalAngewandte Chemie - International Edition
Volume42
Issue number13
DOIs
StatePublished - Apr 4 2003

Keywords

  • Amino acids
  • Beta-peptides
  • Conformational analysis
  • Peptidomimetics
  • Secondary structure

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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