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 language | English |
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Pages (from-to) | 11366-11372 |
Journal | Biochemistry |
Volume | 42 |
Issue number | 38 |
DOIs | |
Publication status | Published - 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