Interactions of Complexes of Heparin and a Positively-Charged Protein with GAG-based Hydrogels

摘要

Results indicate that histone release and sequestration is modulated when co-delivered with soluble heparin. When complexed, histone can diffuse more uniformly into 10% hep MAm hydrogels, possibly due to charge shielding. At 100% hep MAm amounts, the distribution of histone alone and in complex begin to resemble each other, suggesting that the immobilized heparin in the hydrogel competes for histone out of the complexes. These results suggest that complexes can be delivered intact to a certain level. Furthermore, there were no significant differences between the amount of complexed histone left from sequestration studies across hydrogel types, indicating that these complexes may have less affinity for the hydrogels. Such results are important when designing delivery devices that rely on electrostatic interactions to release bioactive growth factors at an injury site and are applicable to a variety of GAG-based hydrogel systems.