The behaviors of proteins at interfaces are fundamental determinants of the success of medical devices. Traditionally, protein adsorption has been viewed as the critical predictor for blood compatibility of materials. More specifically, the adsorption of proteins such as fibrinogen for platelet adhesion and FXII for coagulation have been used to assess suitability of materials for blood contacting applications. Recently, there have been increased efforts in understanding the roles that protein function play in this process. These studies show that conformational changes and changes in protein activity can occur at both hydrophilic and hydrophobic interfaces, suggesting that both adsorptive and non-adsorptive protein-surface interactions have biological consequences. Recent studies in our lab have addressed the functional activity of proteins involved in both coagulation and thrombosis. These studies reveal a highly complex environment where activity depends on both surface chemistry and temporal aspects are involved in determining protein activity at interfaces.

Protein activity and thrombosis at biomaterial interfaces

243rd National Meeting (2012)

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