The Reversible Non-covalent Aggregation Into Fibers of PGLa and Magainin 2 Preserves Their Antimicrobial Activity and Synergism

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Dennis Wilkens Juhl
  • Elise Glattard, Université de Strasbourg
  • ,
  • Morane Lointier, Université de Strasbourg
  • ,
  • Panos Bampilis, Université de Strasbourg
  • ,
  • Burkhard Bechinger, Université de Strasbourg, Institut Universitaire de France

Magainin 2 and PGLa are antimicrobial peptides found together in frog skin secretions. When added as a mixture they show an order of magnitude increase in antibacterial activity and in model membrane permeation assays. Here we demonstrate that both peptides can form fibers with beta-sheet/turn signature in ATR-FTIR- and CD-spectroscopic analyses, but with different morphologies in EM images. Whereas, fiber formation results in acute reduction of the antimicrobial activity of the individual peptides, the synergistic enhancement of activity remains for the equimolar mixture of PGLa and magainin 2 also after fibril formation. The biological significance and potential applications of such supramolecular aggregates are discussed.

Original languageEnglish
Article number526459
JournalFrontiers in cellular and infection microbiology
Volume10
ISSN2235-2988
DOIs
Publication statusPublished - 30 Sep 2020
Externally publishedYes

    Research areas

  • amyloid fiber, antimicrobial peptide, gradual release, peptide-lipid interaction, supramolecular assembly

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