Tuesday, 24 May 2005

This presentation is part of: Polymeric Biomaterials Posters

Rheological Characterization of Hydrogels Assembled via Heparin-Peptide Interactions

Le Zhang, Nori Yamaguchi, and Kristi L. Kiick. University of Delaware, Newark, DE

The design of materials in which assembly, mechanical response, and biological properties are controlled by protein-polysaccharide interactions could mimic the biological environment and find use in many biomedical applications. In the investigations reported here, the heparin binding affinity of a variety of heparin binding peptides has been monitored via heparin-sepharose chromatography and surface plasmon resonance (SPR) experiments. Results from these experiments indicate that a heparin-binding peptide that mimics the heparin-binding domain of human platelet factor 4 (PF4) demonstrates higher heparin-binding affinity and heparin association rate when compared to heparin-binding domains of antithrombin III and heparin-interacting protein. Rheological characterization indicates that hydrogels assembled via interactions of LMWH with PF4 exhibit the highest elastic modulus when compared to hydrogels assembled via other LMWH-peptide interactions, which correlates well with chromatography and SPR results. Manipulation of hydrogel physical properties and erosion profiles will provide novel materials for controlled drug delivery and other biomedical applications.

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