The influence of protein adsorption and surface modifying macromolecules on the hydrolytic degradation of a poly(ether-urethane) by cholesterol esterase.

Previous investigations have demonstrated that the inflammatory cell derived enzyme, cholesterol esterase (CE) could degrade polyurethanes (PUs) by hydrolyzing ester and urethane bonds. Studies that have investigated the development of protective coatings for PUs have reported that the polymer degradation of polyester-urethanes (PESUs) can be reduced with the use of fluorine containing surface modifying macromolecules (SMMs). Since these latter studies were carried out in the presence of relatively pure enzyme, it has not been shown if SMMs would still provide an enhanced inhibitory effect if surfaces were pre-exposed to plasma proteins. This would be more representative of the in vivo scenario since protein adsorption would occur before the appearance of monocyte-derived macrophages which would be a primary source of esterase activities. The current investigation has focused on studying the influence of fibrinogen (Fg) as a simple model of protein adsorption in order to assess the effect of CE in combination with protein on polyether-urethane (PEU) surfaces. The materials were prepared with and without SMMs, and were pre-coated with Fg prior to carrying out biodegradation studies. The pre-adsorption of Fg onto the modified and non-modified surfaces provided a significant delay in the hydrolytic action of CE onto the PEU substrates. However, the effect was gone by 70 days and by the 126th day of incubation, both Fg coated and non-Fg coated groups had the same level of degradation. The difference between Fg coated and non-coated substrates was much smaller for materials containing SMMs. In addition, the pre-adsorption of Fg did not alter the SMMs' ability to provide a more biostable surface over the 4 month incubation period. Copyright 2002 Elsevier Science Ltd.