The N-terminal nonapeptide of cephaibols A and C: A naturally occurring example of mismatched helical screw-sense control

Ugo Orcel, Matteo De Poli, Marta De Zotti, Jonathan Clayden*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

10 Citations (Scopus)

Abstract

The N-terminal nonapeptide domain of the fungal nonribosomal peptide antibiotics cephaibol A and cephaibol C (AcPheAib4LeuIvaGly- Aib) is reported to adopt a right-handed helical conformation in the crystalline state. However, this conformation is at odds with the left-handed helicity observed in solution in related synthetic oligomers capped with Ac-L-PheAib4 fragments. We report the synthesis of four diastereoisomers of the cephaibol N-terminal nonapeptide, and show by NMR and CD spectroscopy that the peptide containing the chiral amino acids Phe and Leu in the naturally occurring relative configuration exists in solution as an interconverting mixture of helical screw-sense conformers. In contrast, the nonapeptide containing the unnatural relative configuration at Phe and Leu adopts a single, stable helical screw-sense, which is left handed when the N-terminal Phe residue is L and right-handed when the N-terminal Phe residue is D.

Original languageEnglish
Pages (from-to)16357-16365
Number of pages9
JournalChemistry - A European Journal
Volume19
Issue number48
Early online date9 Oct 2013
DOIs
Publication statusPublished - 25 Nov 2013

Keywords

  • conformation
  • foldamers
  • NMR spectroscopy
  • peptaibiotics
  • peptides

Fingerprint

Dive into the research topics of 'The N-terminal nonapeptide of cephaibols A and C: A naturally occurring example of mismatched helical screw-sense control'. Together they form a unique fingerprint.

Cite this