Abstract
The adsorption behavior of human plasma fibronectin at physiological pH and ionic strength was investigated by in situ ellipsometry on silica substrates of two different surface energies. The silica substrate was characterized by ellipsometry, galvanic potential, and critical surface tension measurements. Adsorption isotherms in the low concentration range for fibronectin were compared with human fibrinogen and found to be qualitatively similar with increased amounts of protein adsorbed at the plateau on a hydrophobic surface as compared to a hydrophilic one. Reversibility for fibronectin upon dilution was found to be small on a hydrophobic surface while a partial desorption was found on a hydrophilic one. Interaction of antibodies with preadsorbed fibronectin suggests that fibronectin adsorbs in different conformations and/or arrangements on the two types of surfaces. The lectin Concanavalin A and its interaction with preadsorbed fibronectin was also investigated.
Published Version
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