The peptide antibiotic clavanin A interacts strongly and specifically with lipid bilayers.
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.
D000900:Anti-Bacterial Agents / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*; D001798:Blood Proteins / Q000138:chemical synthesis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002152:Calorimetry, Differential Scanning; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism*; D018625:Microscopy, Atomic Force; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010455:Peptides; D010713:Phosphatidylcholines / Q000378:metabolism; D013696:Temperature
D000900:Anti-Bacterial Agents; D001798:Blood Proteins; D008051:Lipid Bilayers; D010455:Peptides; D010713:Phosphatidylcholines; C106713:clavanin A