title: Relaxation processes in the adsorption of surface layer proteins to lipid membranes.
abstract: The present work evaluates the kinetics of the interaction of S-layer protein from Lactobacillus brevis with lipid monolayers by measuring the changes in the surface pressure as a function of time for different lipid compositions and at different lateral compressions. At high surface pressures, or at high cholesterol ratios, in which membrane rigidity and surface polarity are increased, the kinetics can be described by a pure diffusional process. At low pressures or in the absence of cholesterol, the kinetics of protein interaction can be interpreted as a consequence of a relaxation process of the membrane structure coupled to diffusion. As the less packed monolayers are more hydrated, the relaxation processes at low initial surface pressures could be ascribed to changes in water organization in the membrane. These observations denote that kinetic insertion of proteins can be modulated by components that modify the hydration state of the interface.
authors.affiliation: Laboratorio de Microbiología Molecular, DCyT, Universidad Nacional de Quilmes, Roque Sáenz Peña 352, Bernal, Argentina.
authors.forename: Axel
authors.initials: A
authors.lastname: Hollmann
authors.forename: Lucrecia
authors.initials: L
authors.lastname: Delfederico
authors.forename: Graciela
authors.initials: G
authors.lastname: De Antoni
authors.forename: Liliana
authors.initials: L
authors.lastname: Semorile
authors.forename: Edgardo Aníbal
authors.initials: EA
authors.lastname: Disalvo
mesh_terms: D000327:Adsorption; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008563:Membrane Lipids / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D008562:Membrane Glycoproteins; D008563:Membrane Lipids; C055764:S-layer proteins