Elucidating the conformational behavior and membrane-destabilizing capability of the antimicrobial peptide ecPis-4s

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...

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Veröffentlicht in:	Biophysical chemistry 2025-02, Vol.317, p.107353, Article 107353
Hauptverfasser:	de Souza, K.R., Nunes, L.O., Salnikov, E.S., Mundim, H.M., Munhoz, V.H.O., Lião, L.M., Aisenbrey, C., Resende, J.M., Bechinger, B., Verly, R.M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - metabolism Antimicrobial Cationic Peptides - pharmacology Antimicrobial peptides Antimicrobial Peptides - chemistry Antimicrobial Peptides - metabolism Antimicrobial Peptides - pharmacology Cell Membrane - chemistry Cell Membrane - metabolism Conformational analysis of peptides Lipid Bilayers - chemistry Lipid Bilayers - metabolism Membrane active peptides Micelles Nuclear Magnetic Resonance, Biomolecular Peptide topology Peptide-membrane interaction Phosphatidylcholines - chemistry Phosphatidylglycerols - chemistry Piscidins peptides Protein Conformation
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