Mixed β 23-hexapeptides and β 23-nonapeptides folding to (P)-helices with alternating twelve- and ten-membered hydrogen-bonded rings

Magnus Rueping, Jürg V. Schreiber, Gérald Lelais, Bernhard Jaun*, Dieter Seebach

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

90 Scopus citations

Abstract

The structural properties of four mixed β-peptides with alternating β 23- or β 32-sequences have been analyzed by two-dimensional homonuclear 1H-NMR- and CD spectroscopic measurements. All four β-peptides fold into (P)-helices with twelve- and ten-membered H-bonded rings (Figs. 3-6). CD Spectra (Fig. 2) of the mixed β 32-hexapeptide 4a and β 32 -nonapeptide 5a, indicating that peptides of this type also adopt the 12/10-helical conformation, were confirmed by NMR structural analysis. For the deprotected β 32-nonapeptide 5d, NOEs not consistent with the 10/12 helix have been observed, showing that the stability of the helix decreases upon N-terminal deprotection. From the NMR structures obtained, an idealized helical-wheel representation was generated (Fig. 7), which will be used for the design of further 12/10 or 10/12 helices.

Original languageEnglish (US)
Pages (from-to)2577-2593
Number of pages17
JournalHelvetica Chimica Acta
Volume85
Issue number9
DOIs
StatePublished - Oct 29 2002

ASJC Scopus subject areas

  • Catalysis
  • Biochemistry
  • Drug Discovery
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

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