Structure and Dynamics of the Magainin 2 Antimicrobial Peptide in Biomimetic Lipid Bilayers by Solid-State NMR
Year: 2025
Type: article
Abstract: C chemical shift analysis reveals α-helical conformations, the NMR line shapes indicate pronounced conformational heterogeneity, which can be explained by the existence of higher order arrangements along the membrane surface. A reduced degree of helicity is observed when the membrane is in the gel phase suggesting more superficial interactions of magainin 2. Notably, our NMR data show that membrane-associated magainin 2 can evolve into amyloid-like β-sheet structures, forming large peptide-lipid aggregates. This behavior occurs only in bacterial and not in mammalian membrane models, paving the way for a new understanding of the role of these supramolecular assemblies in host defense mechanisms, and highlighting a potential relationship between antimicrobial peptides and functional amyloid structures.
Source: Biochemistry
Authors: Ahmad Saad, Jesus Raya, Burkhard Bechinger
Language: English
Subfield: Microbiology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: green
Awards: Par-delà les frontières, l'Université de Strasbourg, Engineering antibacterial cationic amphipathic peptidomimetics for targeting biofilm-embedded and intracellular bacteria, Apolipoprotein AI Mimetic Peptide lipid Asemblies, G5421051960, New Antibiotics Tackling mUlti-Resistance by acting on Alternative bacteriaL tARgets in Synergy with mEmbrane-disruptiNg AntimicrobiaL peptides., Synergistic action of a photosensitizer and antimicrobial peptides for superbugs destruction
OpenAlex ID: W4414687075