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Highly synergistic antimicrobial activity of magainin 2 and PGLa peptides is rooted in the formation of supramolecular complexes with lipids

Aisenbrey, C.; Amaro, M.; Pospíšil, P.; Hof, M.; Bechinger, B.

Magainin 2 and PGLa are cationic, amphipathic antimicrobial peptides which when added as equimolar mixture exhibit a pronounced synergism in both their antibacterial and pore-forming activities. Here we show for the first time that the peptides assemble into defined supramolecular structures along the membrane interface. The resulting mesophases are quantitatively described by state-of-the art fluorescence self-quenching and correlation spectroscopies. Notably, the synergistic behavior of magainin 2 and PGLa correlates with the formation of hetero-domains and an order-of-magnitude increased membrane affinity of both peptides. Enhanced membrane association of the peptide mixture is only observed in the presence of phophatidylethanolamines but not of phosphatidylcholines, lipids that dominate bacterial and eukaryotic membranes, respectively. Thereby the increased membrane-affinity of the peptide mixtures not only explains their synergistic antimicrobial activity, but at the same time provides a new concept to increase the therapeutic window of combinatorial drugs.

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Verlagsausgabe §
DOI: 10.5445/IR/1000122782
Veröffentlicht am 21.08.2020
DOI: 10.1038/s41598-020-68416-1
Zitationen: 4
Web of Science
Zitationen: 4
Zitationen: 4
Cover der Publikation
Zugehörige Institution(en) am KIT Center for Functional Nanostructures (CFN)
Institut für Angewandte Physik (APH)
Publikationstyp Zeitschriftenaufsatz
Publikationsdatum 15.07.2020
Sprache Englisch
Identifikator ISSN: 2045-2322
KITopen-ID: 1000122782
Erschienen in Scientific reports
Verlag Nature Research
Band 10
Heft 1
Seiten Art. Nr.: 11652
Nachgewiesen in Web of Science
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