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The peptide antibiotic clavanin A interacts strongly and specifically with lipid bilayers
Ellen J M van Kan1, Dragomir N Ganchev, Margot M E Snel
1Department of Functional Ingredients, Food and Food Processing, Agrotechnological Research Institute, Wageningen University and Research Centre, Bornsesteeg 59, 6708 PD Wageningen, The Netherlands.
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.