The peptide antibiotic Clavanin A interacts strongly and specifically with lipid bilayers

E.J.M. van Kan, D.N. Ganchev, M.M.E. Snel, V. Chupin, A. van der Bent, B. de Kruijff

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    31 Citations (Scopus)

    Abstract

    In this study the interaction of the antimicrobial peptide clavanin A with phosphatidylcholine bilayers is investigated by DSC, NMR, and AFM techniques. It is shown that the peptide interacts strongly and specifically with the lipids, resulting in increased order-disorder phase transition temperatures, phase separation, altered acyl chain and headgroup packing, and a drastically changed surface morphology of the bilayer. These results are interpreted in terms of clavanin-specific interactions with lipids and are discussed in the light of the different mechanisms by which clavanin A can destroy the barrier function of biological membranes
    Original languageEnglish
    Pages (from-to)11366-11372
    JournalBiochemistry
    Volume42
    Issue number38
    DOIs
    Publication statusPublished - 2003

    Keywords

    • helical antimicrobial peptides
    • nuclear-magnetic-resonance
    • differential scanning calorimetry
    • x-ray-diffraction
    • phosphatidylcholine bilayers
    • model membranes
    • transmembrane peptides
    • biological-membranes
    • tunicate hemocytes
    • flanking residues

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    van Kan, E. J. M., Ganchev, D. N., Snel, M. M. E., Chupin, V., van der Bent, A., & de Kruijff, B. (2003). The peptide antibiotic Clavanin A interacts strongly and specifically with lipid bilayers. Biochemistry, 42(38), 11366-11372. https://doi.org/10.1021/bi0349017