Fiche publication
Date publication
novembre 2024
Journal
Biophysical chemistry
Auteurs
Membres identifiés du Cancéropôle Est :
Pr BECHINGER Burkhard
Tous les auteurs :
de Souza KR, Nunes LO, Salnikov ES, Mundim HM, Munhoz VHO, Lião LM, Aisenbrey C, Resende JM, Bechinger B, Verly RM
Lien Pubmed
Résumé
Here we present studies of the structure and membrane interactions of ecPis-4 s, a new antimicrobial peptide from the piscidin family, which shows a wide-range of potential biotechnological applications. In order to understand the mode of action ecPis-4 s, the peptide was chemically synthesized and structural investigations in the presence of anionic POPC:POPG (3:1, mol:mol) membrane and SDS micelles were performed. CD spectroscopy demonstrated that ecPis-4 s has a high content of helical structure in both membrane mimetic media, which is in line with solution NMR spectroscopy that revealed an amphipathic helical conformation throughout the entire peptide chain. Solid-state NMR experiments of ecPis-4 s selectively labeled with N/H and reconstituted into uniaxially oriented POPC:POPG membranes revealed an ideal partition of hydrophilic and hydrophobic residues within the bilayer interface. The peptide aligns in parallel to the membrane surface, a topology stabilized by aromatic side-chain interactions of the Phe-1, Phe-2 and Trp-9 with the phospholipids. H NMR experiments using deuterated lipids revealed that anionic lipid accumulates in the vicinity of the cationic peptide upon peptide-membrane binding.
Mots clés
Antimicrobial peptides, Conformational analysis of peptides, Membrane active peptides, Peptide topology, Peptide-membrane interaction, Piscidins peptides
Référence
Biophys Chem. 2024 11 14;317:107353
