Contact
    Start Publications Interaction of a laminin derived peptide with phosphatidyl ...
    ←  Publication Finder
    Attension

    Interaction of a laminin derived peptide with phosphatidyl choline/phosphatidyl glycerol

    Year: 2003

    Journal: Talanta 60 (2003) 591-600, 20111221

    Authors: F. Reig , P. Sospedra , A. Juve , L. Rodriguez

    Organizations: a Department of Peptides, Institute for Biological and Environmental Chemistry, Jordi Girona 18, 08034 Barcelona, Spain b Physicochemical Department, Faculty of Pharmacy, University of Barcelona, Avgda. Joan XXIII s/n, 08028 Barcelona, Spain c Pharmacology Department, Faculty of Medicine, Casanova 143, 08018 Barcelona, Spain

    The physicochemical interactions between an active peptide sequence derived from laminin and phospholipids have been studied. The main aim is to determine the suitability of this peptide fragment to be linked to liposome's with the purpose to develop targeting devices. Results indicate that this peptide is able to insert in lipid monolayers and also to form monomolecular layers at an air/water interface. Besides, miscibility studies carried out through compression isotherms of mixed monolayers [dipalmitoyl phosphatidylcholine (DPPC)/peptide], indicate a strong interaction at 60 - 80% DPPC molar composition. Studies carried out with lipid bilayers indicate that the interaction is restricted to the external face of the vesicles. Moreover, the presence of this peptide in the incubation media promotes a low level of carboxyfluorescein (CF) leakage and no fusion of vesicles. These results indicate that the association of this sequence to vesicles do not produce damage of the bilayer and can be used as potential targeting vector.