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    The affinity of two antimicrobial peptides derived from bovine milk proteins for model lipid membranes

    Year: 2009

    Journal: Colloids and Surfaces A: Physicochemical and Engineering Aspects, Volume 343, Issues 1-3, 10 July 2009, Pages 104-110, 20111221

    Authors: Wanda Barzyka, Sylvie Campagnab, Katarzyna Wieclawc, Beata Korchowiecc, d and Ewa Rogalska

    Organizations: Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239 Krakow, Poland, URAFPA, Nancy-Université, INRA, Equipe Protéolyse-Biofonctionnalité des Protéines et des Peptides, Boulevard des Aiguillettes, BP239, 54506 Vandoeuvre-lès-Nancy, France, Department of Physical Chemistry and Electrochemistry, Faculty of Chemistry, Jagiellonian University, ul. Romana Ingardena 3, 30-060 Krakow, Poland, Structure et Réactivité des Systèmes Moléculaires Complexes, BP 239, CNRS/Nancy Université, 54506 Vandoeuvre-lès-Nancy cedex, France

    In this work, two antimicrobial peptides were studied regarding their capacity to interact with lipid membranes. The peptides subsequently named L-16-Y and N-23-T were derived from the bovine milk α-s2 casein and from the component-3 of proteose peptone (PP3), respectively. 1,2-Dipalmitoyl-sn-glycero-3-phosphocholine (DPPG) and 1,2-dipalmitoyl-sn-glycero-3-phospho-rac-(1-glycerol) (DPPC) monomolecular films spread at the air–water interface were used, respectively, as model host and bacterial membranes. The surface pressure and surface potential measurements, as well as Brewster angle microscopy (BAM) showed that both peptides interact with the model membranes. However, the higher affinity for DPPG compared to DPPC indicates that these peptides are innocuous for the host membranes.