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

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)9802-9810
Number of pages9
JournalJournal of Physical Chemistry B
Volume113
Issue number29
DOIs
StatePublished - 23 Jul 2009
Externally publishedYes

Fingerprint

Dive into the research topics of 'Interaction of the cationic peptide bactenecin with phospholipid monolayers at the air - Water interface: I interaction with 1,2-dipalmitoyl-sn-glycero-3- phosphatidilcholine'. Together they form a unique fingerprint.

Cite this