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Softening of POPC membranes by magainin
Authors:Hélène Bouvrais  Philippe Méléard  Tanja Pott  Knud J Jensen  Jesper Brask  John H Ipsen
Institution:1. Department of Physics and Chemistry, MEMPHYS-Center for Biomembrane Physics, University of Southern Denmark, Odense, Denmark;2. UMR-CNRS 6510, Université de Rennes 1, Rennes, France;3. Department of Natural Sciences, Section for Bioorganic Chemistry, University of Copenhagen, Frederiksberg, Denmark
Abstract:Magainin 2 belongs to the family of peptides, which interacts with the lipid membranes. The present work deals with the effect of this peptide on the mechanical properties of 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine Giant Unilamellar Vesicle, characterized by the bending stiffness modulus. The bending elastic modulus is measured by Vesicle Fluctuation Analysis at biologically relevant pH and physiological buffer conditions and shows a dramatic decrease with increasing peptide concentration. The observed bilayer softening is interpreted in terms of a continuum model describing perturbations on the membrane organization. Our analysis suggests that the adsorbed peptides give rise to considerable local curvature disruptions of the membrane.
Keywords:Lipid bilayer  Vesicle fluctuation analysis  Membrane mechanics  Magainin  Bending elasticity  Continuum model
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