Generalised bilayer perturbation from peptide helix dimerisation at membrane surfaces: Vesicle lysis induced by disulphide-dimerised melittin analogues

Jiro Takei, Attila Remenyi, Christopher E. Dempsey

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The effects of covalent dimerisation of melittin by disulphide formation in cysteine-substitution analogues, (melittin K23C)2 and (melittin K23Q,Q25C)2, on the kinetics of pore formation in phosphatidylcholine small unilamellar vesicles was measured under low ionic strength conditions. The initial rate of melittin-induced pore formation increased with the square of the peptide concentration, whereas both disulphide-dimerised melittin analogues showed a first-order dependence of pore formation rates on peptide concentration. These results indicate that peptide dimerisation is rate-limiting for pore formation under these conditions. A model for a generalised bilayer perturbation resulting from the self-association of a pair of peptide helices at the membrane surface is proposed which may have implications for a number of biological processes that involve the interaction of helical polypeptides with membranes. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)11-14
Number of pages4
JournalFEBS letters
Issue number1
Publication statusPublished - Jan 8 1999



  • Colicin
  • Magainin
  • Membrane protein
  • Peptide antibiotic
  • Sec-independent

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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