Nonfouling biomaterials based on polyethylene oxide-containing amphiphilic triblock copolymers as surface modifying additives: Protein adsorption on PEO-copolymer/polyurethane blends Academic Article uri icon

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abstract

  • Surface modification of a segmented polyurethane was achieved by blending with novel PEO-containing amphiphilic triblock copolymers (PEO-polyurethane-PEO). Three copolymers having different PEO MW (550, 2000, 5000) were used as surface modification additives. The protein resistance of the blend surfaces was evaluated using radiolabeling methods. On the blends of copolymers with PEO blocks of MW 2000 and 5000, fibrinogen adsorption from physiologic buffer decreased with increasing copolymer content up to 20 wt%. On the blends with PEO blocks of MW 550, resistance to adsorption for a given copolymer content was much greater. For all three blend types at 20% copolymer content, reductions in adsorption compared to the unmodified PU matrix were greater than 95%. Reductions in adsorption were similar for the 20% blends and surfaces prepared by coating the copolymers directly on the matrix, suggesting that the 20% blend surfaces were completely covered by copolymer. At low copolymer content (< or =10 wt %), fibrinogen adsorption decreased with decreasing PEO block length. This was probably due to increasing surface coverage of the copolymers with decreasing block length. It is therefore concluded that surface density of PEO is more important than PEO MW for the protein resistance of these surfaces. Lysozyme, a much smaller protein, showed adsorption trends similar to fibrinogen. The adsorption of fibrinogen and lysozyme from binary solutions to blends of the copolymer with PEO blocks of 2000 MW was investigated to probe the effects of protein size on adsorption resistance. Fibrinogen and lysozyme showed similar fractional decreases in adsorption relative to the PU matrix independent of the surface density of PEO. However lysozyme was enriched in the surface relative to the solution, that is, it was adsorbed preferentially to fibrinogen.

publication date

  • June 15, 2008