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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