Authors Renner, L. ; Pompe, T. ; Salchert, K. ; Werner, C.
Title Dynamic Alterations of Fibronectin Layers on Copolymer Substrates with Graded Physiochemical Characteristics
Date 30.03.2004
Number 12192
Abstract Desorption and exchange of preadsorbed fibronectin layers in pure buffer solution and solutions ofhuman serum albumin or fibronectin, respectively, were studied in dependence on the physicochemicalcharacteristics of maleic acid copolymer films used as substrates. Although the preadsorbed amount offibronectin differed only slightly, the protein was found to exhibit a significantly enhanced anchorage atthe more hydrophobic polymer surface as compared to the more hydrophilic and more negatively chargedpolymer surface. The preadsorbed fibronectin layer was most efficiently exchanged by fibronectin (i.e., inthe homodisplacement process) while pure buffer solution and human serum albumin solutions induceddesorption or exchange of fibronectin to lower and similar degrees. An increase of the total adsorbedamount of protein due to additional adsorption of fibronectin or human serum albumin accompanied thepartial exchange of the preadsorbed fibronectin in the displacement experiments. Evaluation of the kineticsof desorption and exchange of fibronectin at any of the substrates revealed two kinds of surface-attachedprotein populations-a fast desorbing species and a species with a slow desorption and exchange rate. Bya multivariate regression analysis the surface characteristics of the polymer substrate were confirmed todetermine the degree of protein desorption and exchange while the dynamics of the layer alteration wasfound to solely depend on the diffusion behavior of the proteins.
Publisher Langmuir
Citation Langmuir 20 (2004) 2928-2933
Tags MBC_Matrix , Protein Interactions at Cell Polymer Interfaces

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