Flaws in foldamers: conformational uniformity and signal decay in achiral helical peptide oligomers

Research output: Contribution to journalArticle

  • External authors:
  • B A F Le Bailly
  • L Byrne
  • V Diemer
  • M Foroozandeh
  • J Clayden

Abstract

Although foldamers, by definition, are extended molecular structures with a well-defined conformation, minor conformers must be populated at least to some extent in solution. We present a quantitative analysis of these minor conformers for a series of helical oligomers built from achiral but helicogenic alpha-amino acids. By measuring the chain length dependence or chain position dependence of NMR or CD quantities that measure screw-sense preference in a helical oligomer, we quantify values for the decay constant of a conformational signal as it passes through the molecular structure. This conformational signal is a perturbation of the racemic mixture of M and P helices that such oligomers typically adopt by the inclusion of an N or C terminal chiral inducer. We show that decay constants may be very low (

Bibliographical metadata

Original languageEnglish
Pages (from-to)2313-2322
Number of pages10
JournalChemical Science
Volume6
Issue number4
DOIs
StatePublished - 2015