Different pathways of bilayer disruption by the structurally related antimicrobial peptides cecropin B, B1 and B3, revealed by surface plasma resonance analysis of immobi-lized liposomes, differential scanning calorimetryof peptide– large unilamellar vesicle interactions, and light microscopic analysis of peptide-treated giant unilamellar vesicles, have been identified inthis cecropinB(CB)hasone amphipathic and one hydrophobica-helix, whereas cecro-pins B1 (CB1) and B3 (CB3), which are custom-designed, chimaeric analogues of CB, possess either two amphipathic or two hydrophobica-helices, respectively
