Design, Synthesis and Structural Investigations of a β-Peptide Forming a 314-Helix Stabilized by Electrostatic Interactions

Magnus Rueping, Yogesh R. Mahajan, Bernhard Jaun, Dieter Seebach*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

Abstract

Two different strategies have been employed for the synthesis of Fmoc-protected β3-homoarginine; the Arndt-Eistert homologation of α-arginine and the guanidinylation of β3-homoornithine. Solid-phase β-peptide synthesis was used for the preparation of β-heptapeptide 1, which was designed to form a helix stabilized by electrostatic interactions through positively (β3hArg) and negatively charged (β3hGlu) amino acid residues. CD measurements and corresponding NMR investigations in MeOH and aqueous solutions do indeed show that the β-peptidic 314-helix can be stabilized by salt-bridge formation.

Original languageEnglish (US)
Pages (from-to)1607-1615
Number of pages9
JournalChemistry - A European Journal
Volume10
Issue number7
DOIs
StatePublished - Apr 2 2004

Keywords

  • Electrostatic interactions
  • Helical structures
  • NMR spectroscopy
  • Salt bridges
  • β-peptides

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Organic Chemistry

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