The Reversible Non-covalent Aggregation Into Fibers of PGLa and Magainin 2 Preserves Their Antimicrobial Activity and Synergism.
Fiche publication
Date publication
janvier 2020
Journal
Frontiers in cellular and infection microbiology
Auteurs
Membres identifiés du Cancéropôle Est :
Pr BECHINGER Burkhard
Tous les auteurs :
Juhl DW, Glattard E, Lointier M, Bampilis P, Bechinger B
Lien Pubmed
Résumé
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.
Mots clés
amyloid fiber, antimicrobial peptide, gradual release, peptide-lipid interaction, supramolecular assembly
Référence
Front Cell Infect Microbiol. 2020 ;10:526459