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    Bacteriocin enterocin CRL35 is a modular peptide that induces non-bilayer states in bacterial model membranes

    Year: 2020

    Journal: Biochim. Biophys. Acta-Biomembr., Volume 1862, FEB 1

    Authors: Aniado, CM; Minahk, CJ; Cilli, E; Oliveira, RG; Dupuy, FG

    Organizations: Agencia Nacional de Promocion Cientifica y Tecnologica (ANPCyT), FONCYT, ArgentinaANPCyTFONCyT [3563, 0819]; LNLS-CNPeM [20170143]; Concejo Interuniversitario Nacional (CIN), Argentina

    Keywords: Bacteriocin; Bacterial membrane; Listeria; X-ray diffraction; Monolayer; Spectroscopy

    The mechanism of action of the anti-Listeria peptide enterocin CRL35 was studied with biophysical tools by using lipid mixtures that mimicked Gram-positive plasma membranes. Langmuir monolayers and infrared spectroscopy indicated that the peptide readily interacted with phospholipid assembled in monolayers and bilayers to produce a dual effect, depending on the acyl chains. Indeed, short chain mixtures were disordered by enterocin CRL35, but the gel-phases of membranes composed by longer acyl chains were clearly stabilized by the bacteriocin. Structural and functional studies indicated that non-bilayer states were formed when liposomes were co-incubated with enterocin CRL35, whereas significant permeabilization could be detected when bilayer and non-bilayer states co-existed. Results can be explained by a two-step model in which the N-terminal of the peptide firstly docks enterocin CRL35 on the lipid surface by means of electrostatic interactions; then, C-terminal triggers membrane perturbation by insertion of hydrophobic alpha-helix.
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