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

Ivan V. Korendovych, Scott J. Shandler, Geronda L. Montalvo, William F. Degrado

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

Transmembrane (TM) β-peptides comprised of acyclic β3-amino acids demonstrate equilibrium between 12- and 14-helical structures in an environment- and sequence-dependent manner. Circular dichroism (CD) spectra of TM β3-peptides may be described as linear combinations of the 12- and 14-helical CD spectra. The apparent malleability of β3-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.

Original languageEnglish (US)
Pages (from-to)3474-3477
Number of pages4
JournalOrganic Letters
Volume13
Issue number13
DOIs
StatePublished - Jul 1 2011

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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