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Show 64 Kristen Kurtzeborn college of pharmacy Catheter-associated thrombosis is a major issue for kidney dialysis patients. Currently, anti-coagulation patient prophylaxis to implanted catheter materials uses systemic heparins and heparin-coated materi-als. Unfortunately, these approaches do not sufficiently address the clinical problems with catheters. Once surface-bound heparin on an implant is depleted or buried under the host's protein and coagula-tion response, the biomaterial can no longer adequately prevent coagulation. Furthermore, repeated patient exposure to exogenous heparin can lead to several side effects, culminating in an increased risk of thrombosis. To address this issue, a recombinant spider silk-based coating is being developed to provide a durable, "rechargeable" heparin-binding catheter coating. Spider silk, recognized for its biocompatibility and mechanical properties, has been genetically polymerized with a conserved heparin binding domain (HBD) to endow it with new anticoagulation properties in the context of its durable, protease-resistant properties. However, to understand the capabilities for spider silk peptide domains with heparin binding capabilities, silk's inherent heparin interactions must be assessed. Column affinity chromatography has been performed with Heparin HyperD® Resin 2.2.3.1 (Pall Corporation) to determine the binding affinity between silk and heparin. Comparison of fractional elution profiles with anti-thrombin III (ATIII), a known high affinity heparin-binding component in the blood coagulation cascade, provides a method for ac-curate assessment of the inherent heparin-binding capability of an Argiope aurantia-based silk domain. Further studies will use the column chromatography methods developed here to determine the ability of the small, conserved HBD to bind heparin when recombinantly expressed with the spider silk domain. The goal is to create a biomaterial with the capacity to bind heparin, maintain thromboresistance in blood and be reloaded with heparin on demand. ASSESSING BINDING AFFINITY BETWEEN RECOMBINANT ARGIOPE AURANTIA SILK PROTEIN AND HEPARIN Kristen Kurtzeborn, (Dorina Diekjürgen, David W. Grainger, Amanda E. Brooks) Department of Bioengineering Department of Pharmaceutics and Pharmaceutical Chemistry University of Utah UNDERGRADUATE RESEARCH ABSTRACTS Dorina Diekjürgen David W. Grainger Amanda E. Brooks |
