Although it is widely believed that blood compatibility is primarily determined by the amount of fibrinogen adsorbed to a biomaterial surface, recent results in our laboratory have shown that platelet adhesion does not generally correlate with the amount of adsorbed fibrinogen but with the degree of biomaterial-induced protein unfolding. Our studies have shown that platelets will even readily adhere to adsorbed albumin through this mechanism.  We have further proved that platelet adhesion to albumin is actually receptor mediated, even though albumin has no known platelet binding sites. We hypothesize that the mechanism responsible for this behavior is the pulling apart of salt bridges between oppositely charged amino acid residues, such as arginine and aspartic acid, thus creating RGD-like motifs and that this is a universal response for all proteins. In this talk I will present our experimental results that support these hypotheses and their implications for biomaterial surface design.

Biomaterial-induced protein unfolding as a universal mechanism controlling blood compatibility

245th National Meeting (2013)

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