Interaction of the cationic peptide bactenecin with mixed phospholipid monolayers at the air-water interface

Ana B. López-Oyama, Pablo Taboada, María G. Burboa, Ezequiel Rodríguez, Víctor Mosquera, Miguel A. Valdez*

*Autor correspondiente de este trabajo

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

18 Citas (Scopus)

Resumen

The initial mechanism by which antimicrobial peptides target microbes occurs via electrostatic interactions; however, the mechanism is not well understood. We investigate the interaction of the antimicrobial peptide bactenecin with a 50:50. w:w% 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dimyristoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (DMPG) phospholipid mixture at the air-water interface with different NaCl concentrations (0.01, 0.05, 0.1, 0.5. M) in the subphase. A larger shift of DPPC:DMPG isotherms was obtained for 0.1. M salt concentration at lower and higher pressures, demonstrating the influence of the negative charge of DMPG molecules and the screening of the electrostatic interaction by the salt concentration. Raman spectroscopy of monolayers demonstrated the presence of cysteine-cysteine bridges in bactenecin loops. The peptide adsorption in DPPC:DMPG monolayers observed by AFM images suggests a self-assembled aggregation process, starting with filament-like networks. Domains similar to carpets were formed and pore structures were obtained after a critical peptide concentration, according to the carpet model.

Idioma originalInglés
Páginas (desde-hasta)279-288
Número de páginas10
PublicaciónJournal of Colloid and Interface Science
Volumen359
N.º1
DOI
EstadoPublicada - 1 jul. 2011

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