Artificial ion channels formed by a synthetic cyclic peptide

D. Wang, L. Guo, J. Zhang, R. W. Roeske, L. R. Jones, Z. Chen, C. Pritchard

Research output: Contribution to journalArticle

38 Scopus citations

Abstract

A new cyclic peptide 1 having an (LLLD)3 configuration pattern was designed that is capable of forming artificial transmembrane ion channels by self-assembly of planar peptide rings, with hydrophilic groups arrayed in the interior of the channel. Ion permeability in the presence of the synthetic peptide 1, cyclo[-Trp-Dap-LeU-D-Ala-Trp-Ser-Val-D-Ala-Trp-Ser-Ile-Gly-] (Dap: L-diaminopropionic acid), was observed in lipid bilayer membranes. The pH dependence of ionic conductance showed that the β-amino group of Dap may play a role in the conductance of the peptide channels. Fourier-transform infrared and circular dichroism data imply that, in a membrane, a stack of cyclic peptides is formed in which the inter peptide H bonds form a kind of β-structure analogous to that in the gramicidin A dimer and distinct from the H-bonding pattern of the β-barrels.

Original languageEnglish (US)
Pages (from-to)301-306
Number of pages6
JournalJournal of Peptide Research
Volume57
Issue number4
DOIs
StatePublished - Aug 29 2001

Keywords

  • β-sheet conformation
  • Ion channels
  • Lipid bilayers
  • Self-assembly
  • Synthetic cyclic peptides

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

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