Environment- and sequence-dependence of helical type in membrane-spanning peptides composed of β3-amino acids

Org Lett. 2011 Jul 1;13(13):3474-7. doi: 10.1021/ol201218y. Epub 2011 Jun 9.


Transmembrane (TM) β-peptides comprised of acyclic β(3)-amino acids demonstrate equilibrium between 12- and 14-helical structures in an environment- and sequence-dependent manner. Circular dichroism (CD) spectra of TM β(3)-peptides may be described as linear combinations of the 12- and 14-helical CD spectra. The apparent malleability of β(3)-substituted acyclic β-peptides has practical implications for foldamer design, as it suggests that both the 14-helix and 12-helix might be reasonable platforms for molecular recognition.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Protein Structure, Secondary
  • Stereoisomerism


  • Amino Acids
  • Peptides