Interaction of the cationic peptide bactenecin with phospholipid monolayers at the air - Water interface: I interaction with 1,2-dipalmitoyl-sn-glycero-3- phosphatidilcholine

A. B. López-Oyama, A. L. Flores-Vázquez, M. G. Burboa, L. E. Gutierrez-Millan, J. Ruiz-García, M. A. Valdez

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15 Citas (Scopus)

Resumen

In this work we have investigated the influence of NaCl on the adsorption of the antimicrobial cationic peptide bactenecin in the monolayer of 1, 2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) at the air-water interface, as a function of NaCl concentrations in the subphase. We show that the effect of the salt concentration on DPPC monolayers is a monotonic decrease of the liquid-condensed-liquid-expanded (LC-LE) coexistence region. By contrast, the effect of the bactenecin adsorption at the DPPC monolayer not only removed the LC-LE coexistence region plateau, but also shifted the DPPC isotherms to higher pressures and increased the compressibility of the DPPC/bactenecin monolayers with respect to the pure DPPC monolayer around the LC phase. Analysis of the domain structure, obtained by Brewster angle and atomic force microscopes, indicates that the salt concentration in the subphase builds an electrostatic barrier, increasing the rigidity of DPPC monolayers and limiting the bactenecin adsorption at the LC-LE phase coexistence.

Idioma originalInglés
Páginas (desde-hasta)9802-9810
Número de páginas9
PublicaciónJournal of Physical Chemistry B
Volumen113
N.º29
DOI
EstadoPublicada - 23 jul. 2009
Publicado de forma externa

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