INVESTIGADORES
MINAHK Carlos Javier
artículos
Título:
Bacteriocin enterocin CRL35 is a modular peptide that induces non-bilayer states in bacterial model membranes
Autor/es:
AMADO, CAROLINA MEDINA; MINAHK, CARLOS J.; CILLI, EDUARDO; OLIVEIRA, RAFAEL G.; DUPUY, FERNANDO G.
Revista:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Lugar: Amsterdam; Año: 2020 vol. 1862
ISSN:
0005-2736
Resumen:
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 α-helix.