Influence of Substrate Hydrophobicity on the Adsorption of Collagen in the Presence of Pluronic F68, Albumin, or Calf Serum

The influence of Pluronic F68 [a poly(ethylene oxide)-poly(propylene oxide)-poly(ethylene oxide) copolymer surfactant], serum albumin (HSA), and fetal calf serum (FCS) on the adsorption of type I collagen by polymer substrates was investigated using radiolabeling and XPS analysis. Three different kinds of polystyrene substrates with increasing level of hydrophobicity were used. Change in the state of hydration of the sorbent and protein surfaces appears to be the main driving force for collagen adsorption. Pluronic F68 strongly reduces collagen adsorption, the reduction being more pronounced with higher substrate hydrophobicity. This explains why epithelial cell adhesion on substrates preconditioned with a solution of Pluronic F68 and collagen is strongly influenced by substrate hydrophobicity. Collagen adsorption is also reduced in the presence of HSA and FCS, but the reduction and its sensitivity to substrate hydrophobicity are lower than with Pluronic F68