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

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

Author information

1
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.

Erratum in

  • Org Lett. 2012 Jun 15;14(12):3236.

Abstract

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.

PMID:
21651308
PMCID:
PMC3124938
DOI:
10.1021/ol201218y
[Indexed for MEDLINE]
Free PMC Article

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