Do interstrand hydrogen bonds contribute to β-hairpin peptide stability in solution? IR analysis of peptide folding in water

Christopher S. Colley, Samuel R. Griffiths-Jones, Michael W. George, Mark S. Searle

Research output: Journal PublicationArticlepeer-review

24 Citations (Scopus)

Abstract

The amide I carbonyl stretch in the IR spectrum, together with 1H NMR Hα chemical shifts, have been used to investigate the folding of a 16- residue β-hairpin peptide in water: while Hα shifts are consistent with a significant population of the folded state (ca. 40%), we see no features in the IR spectrum in the amide I region to suggest a significant contribution from interstrand hydrogen bonds, although at high peptide concentration (≥10 mM) the appearance of a new band at 1616 cm-1 is consistent with the onset of irreversible peptide aggregation.

Original languageEnglish
Pages (from-to)593-594
Number of pages2
JournalChemical Communications
Issue number7
DOIs
Publication statusPublished - 7 Apr 2000
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Chemistry (all)
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

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