Reversible α-helix formation controlled by a hydrogen bond surrogate

Stephen E. Miller, Neville R. Kallenbach, Paramjit S. Arora

Research output: Contribution to journalArticlepeer-review


Strategically placed covalent linkages have been shown to stabilize helical conformations in short peptide sequences. Here we report the synthesis of a stabilized α-helix that utilizes an internal disulfide linkage. Structural analysis indicates that the dynamic nature of the disulfide bridge allows for the reversible formation of an α-helix through oxidation and reduction reactions.

Original languageEnglish (US)
Pages (from-to)4434-4437
Number of pages4
Issue number23
StatePublished - Jun 10 2012


  • Disulfide bridge
  • Foldamer
  • Helix inducer
  • Hydrogen bond surrogate
  • Stabilized α-helix

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry


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