A differential scanning calorimetry study of the effects and interactions of antimicrobial peptide LS3 on phosphatidylethanolamine bilayers

Farid Sa'adedin, Jeremy P. Bradshaw

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1 Citation (Scopus)


Differential Scanning Calorimetry studies of a synthetic peptide revealed the peptide decreased the temperature of the lamellar-hexagonal phase transition of cis-trans mixtures of phosphatidylethanolamine. The transition enthalpy varied significantly with lipid composition. The findings are discussed with reference to peptide saturation on the bilayer surface, bilayer thinning and peptide orientation.

Original languageEnglish
Pages (from-to)1345-1350
Number of pages6
JournalProtein and Peptide Letters
Issue number11
Publication statusPublished - 1 Jan 2010


  • Amphipathic helix
  • Antimicrobial peptide
  • DSC
  • LS3
  • Phase transition
  • Phosphatidylethanolamine

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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