Autor(es): Medina Amado, Carolina ; Minahk, Carlos J. ; Cilli, Eduardo [UNESP] ; Oliveira, Rafael G. ; Dupuy, Fernando G.
Data: 2020
Identificador Persistente: http://hdl.handle.net/11449/201338
Origem: Oasisbr
Assunto(s): Bacterial membrane; Bacteriocin; Listeria; Monolayer; Spectroscopy; X-ray diffraction; Bacterial membrane; Bacterial membrane; Bacteriocin; Bacteriocin; Listeria; Listeria; Monolayer; Monolayer; Spectroscopy; Spectroscopy; X-ray diffraction; X-ray diffraction
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Agencia Nacional de Promoción Científica y Tecnológica
Fondo para la Investigación Científica y Tecnológica
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.
Instituto Superior de Investigaciones Biológicas (INSIBIO) CONICET-UNT and Instituto de Química Biológica “Dr Bernabé Bloj” Facultad de Bioquímica Química y Farmacia Universidad Nacional de Tucumán, Chacabuco 461
Instituto de Química UNESP Universidad Estadual Paulista, Rua Prof. Francisco Degni, 55 Araraquara
Instituto de Investigaciones en Química Biológica de Córdoba (CIQUIBIC) CONICET-Departamento de Química Biológica Ranwel Caputto Facultad de Ciencias Químicas Universidad Nacional de Córdoba, Haya de la Torre y Medina Allende, Ciudad Universitaria
Instituto de Química UNESP Universidad Estadual Paulista, Rua Prof. Francisco Degni, 55 Araraquara
Fondo para la Investigación Científica y Tecnológica: 0819
Fondo para la Investigación Científica y Tecnológica: 3563
