Abstract
AbstractPlasma polymer coatings are widely applied to the modification of biomaterial surfaces. In order to understand the role of the surface in the adhesion of cells to these materials, it is necessary to understand how protein adsorption is influenced by the plasma polymer surface chemistry. In coated scaffolds, plasma polymerised allylamine has been found to encourage fibroblast adhesion while plasma polymerised hexane reduces cell adhesion. To study the role of proteins in this process, albumin and fibronectin are pre‐adsorbed individually, competitively or sequentially to the plasma polymer surfaces before seeding them with a culture of 3T3 fibroblasts. Significant dependence upon the protein pre‐adsorption was seen in the adhered cell numbers. In situ measurements of protein adsorption using a quartz crystal microbalance help to elucidate the factors that govern the observed cellular response. The measured protein adsorption is rationalised in terms of our knowledge of the surface chemistry of these plasma polymers. We found that high cell adhesion is related to the ability of fibronectin to displace albumin. This ability is reduced on the hydrophobic plasma polymer as well as by adsorbing albumin and fibronectin sequentially.magnified image
Published Version
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