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Biologische Systeme und Medizin Poster: Mi., 14:00–16:30 M-P197<br />

The interaction of antimicrobial peptides with model membranes investigated<br />

by small angle X-ray scattering<br />

Sebastian Linser 1 , Sergio S. Funari 2 , Regine Willumeit 1<br />

1 GKSS Research Center, Max-Planck-Str. 1, 21502 Geesthacht, Germany –<br />

2 Hasylab@DESY, Notkestr. 85, 22603 Hamburg, Germany<br />

The uprising resistance of pathogenic bacteria is a severe problem in health care. To<br />

develop new antibiotic treatment, naturally occurring antimicrobial peptides and synthetic<br />

derivates might become potent agents. These peptides have a direct physical<br />

impact on the membranes of their target cells and display selectivity for bacteria and<br />

fungi in contrast to mammalian cells. In our work we tested the antibacterial activity<br />

of the synthetic peptide NK-CS and derivatives thereof against E. coli (Gram negative)<br />

and S. carnosus (Gram positive) bacteria as well as the hemolytic properties against<br />

human erythrocytes to determine the selectivity of the peptides. In parallel we investigated<br />

the interaction of the peptides with different model membranes, mimicking<br />

bacterial and human membranes, by small angle X-ray scattering (SAXS). The combination<br />

of these techniques gives an indication of the structure-function relationship<br />

of this peptide-lipid-system.<br />

Among the tested peptide, NK-CS was found to be the most potent antimicrobial peptide,<br />

while all derivatives showed less antibacterial selectivity and activity. Structural<br />

characterization of the interaction between the peptides and different model membranes<br />

revealed that the peptides showed no influence on phosphatidylcholine lipids,<br />

representing the membrane of erythrocytes, but for all tested peptides the inverse<br />

hexagonal phase transition of phosphatidylethanolamine lipids, standing for the main<br />

component of the bacterial membrane of E. coli, was significantly altered in a specific<br />

manner which can be correlated with the activity of the peptides. This phase transition<br />

temperature was increased by the peptides promoting a positive curvature of the<br />

membranes eventually leading to the disruption of the model membranes.

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