Authors Renner, L. ; Pompe, T. ; Salchert, K. ; Werner, C.
Title Fibronectin Displacement at Polymer Surfaces
Date 14.06.2005
Number 13102
Abstract The interactions of fibronectin with thin polymer films are studied in displacement experiments usinghuman serum albumin. Fibronectin adsorption and exchange on two different maleic anhydride copolymersurfaces differing in hydrophobicity and surface charge density have been analyzed by quartz crystalmicrobalance and laser scanning microscopy with respect to adsorbed amounts, viscoelastic properties,and conformation. Fibronectin is concluded to become attached onto hydrophilic surfaces as a "softer", lessrigid protein layer, in contrast to the more rigid, densely packed layer on hydrophobic surfaces. As a result,the fibronectin conformation is more distorted on the hydrophobic substrates together with remarkablydifferent displacement characteristics in dependence on the adsorbed fibronectin surface concentrationand the displacing albumin solution concentration. While the displacement kinetic remains constant forthe strongly interacting surface, an acceleration in fibronectin exchange is observed for the weakly interactingsurface with increasing fibronectin coverage. For displaced amounts, no change is determined for thehydrophobic substrate, in contrast to the hydrophilic substrate with a decrease of fibronectin exchangewith decreasing coverage leading finally to a constant nondisplaceable amount of adsorbed proteins.Furthermore, the variation of the albumin exchange concentration reveals a stronger dependence of thekinetic for the weakly interacting substrate with higher rates at higher albumin concentrations.
Publisher Langmuir
Citation Langmuir 21 (2005) 4571-4577
Tags Protein Interactions at Cell Polymer Interfaces

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