A degradable polar hydrophobic ionic polyurethane (D-PHI) has previously been shown to support a less pro-inflammatory monocyte activation relative to tissue culture polystyrene and poly(lactide-co-glycolide). The mechanism by which D-PHI supports this differential response has been evaluated in terms of protein adsorption and surface chemistry in the present study. Surface analysis was performed by X-ray photoelectron spectroscopy (surface chemistry) and water contact angle measurements (surface wettability). The composition of the adsorbed protein layer was probed through 2-D electrophoresis. Protein pre-adsorbed and non-coated D-PHI surfaces were shown to support reduced pro-inflammatory monocyte activation. It was demonstrated that a2-macroglobulin (A2M) supported differential monocyte activation when pre-adsorbed to the above three biomaterials, with the differences showing that the A2M receptor was active on monocytes interacting with A2M pre-adsorbed to D-PHI, but not the two other biomaterials. This study illustrates the importance of protein adsorption in eliciting inflammatory-related biological responses to different biomaterials.

Protein adsorption and monocyte activation on a degradable polar hydrophobic ionic polyurethane

243rd National Meeting (2012)

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