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

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    0531413 - ÚFCH JH 2021 RIV GB eng J - Článek v odborném periodiku
    Aisenbrey, Ch. - Amaro, Mariana - Pospíšil, Petr - Hof, Martin - Bechinger, B.
    Highly synergistic antimicrobial activity of magainin 2 and PGLa peptides is rooted in the formation of supramolecular complexes with lipids.
    Scientific Reports. Roč. 10, č. 1 (2020), č. článku 11652. ISSN 2045-2322. E-ISSN 2045-2322
    Grant CEP: GA ČR(CZ) GX19-26854X
    Institucionální podpora: RVO:61388955
    Klíčová slova: xenopus-laevis * membranes * bilayers * family * model * permeability * enhancement * mechanism * diffusion * topology
    Obor OECD: Physical chemistry
    Impakt faktor: 4.380, rok: 2020
    Způsob publikování: Open access

    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.
    Trvalý link: http://hdl.handle.net/11104/0310078

     
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