Surface induced thrombosis is a major limiting factor in blood contacting devices. Previous in vitro and in vivo work in our laboratory , showed an improved blood compatibility of synthetic materials when physically adsorbed with a recombinant human elastin-like polypeptide (ELP, in particular ELP2). Recently we have shown that the magnitude of platelet adhesion and fibrinogen adsorption to a family of ELPs (ELP1, ELP2 and ELP4), physically adsorbed onto Mylar films, decreased as the ELP sequence length increased, respectively. In the literature, it is unclear as to the mechanism(s) behind elastins' nonthrombogenic behavior. Thus, this work aims to understand the manner in which our family of ELPs improves hemocompatibility by investigating their adsorption properties and how this in turn impacts the interaction with fibrinogen (in terms of configuration and activity).
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