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 o xide)-poly(ethylene oxide) copolymer surfactant], serum albumin (HSA), and fetal calf serum (FCS) on the adsorption of type I collagen by po lymer substrates was investigated using radiolabeling and XPS analysis . Three different kinds of polystyrene substrates with increasing leve l 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 adsorptio n, the reduction being more pronounced with higher substrate hydrophob icity. This explains why epithelial cell adhesion on substrates precon ditioned with a solution of Pluronic F68 and collagen is strongly infl uenced by substrate hydrophobicity. Collagen adsorption is also reduce d in the presence of HSA and FCS, but the reduction and its sensitivit y to substrate hydrophobicity are lower than with Pluronic F68. (C) 19 97 Academic Press.