info:eu-repo/semantics/article
Bacteriocin enterocin CRL35 is a modular peptide that induces non-bilayer states in bacterial model membranes
Fecha
2020-02Registro en:
Medina Amado, Carolina; Minahk, Carlos Javier; Cilli, Eduardo; Oliveira, Rafael Gustavo; Dupuy, Fernando Gabriel; Bacteriocin enterocin CRL35 is a modular peptide that induces non-bilayer states in bacterial model membranes; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1862; 2; 2-2020; 1-36; 183135
0005-2736
CONICET Digital
CONICET
Autor
Medina Amado, Carolina
Minahk, Carlos Javier
Cilli, Eduardo
Oliveira, Rafael Gustavo
Dupuy, Fernando Gabriel
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.