In Situ Photopolymerized Hydrogels for Enhancing Protein Delivery

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Clemson University, 2007 - 337 pages
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Another challenge of using hydrophilic hydrogels for controlled protein delivery is the networks' high permeability to encapsulated proteins. This limitation was circumvented by synthesizing affinity ligands that bind to target proteins and immobilizing them within otherwise inert hydrogel networks (Chapter 5). This modification provided a unique method for tuning the protein delivery rates. Two protein-binding mechanisms, namely electrostatic interaction and metal-ion chelation, were used separately to evaluate the efficacy of protein-ligand binding for controlling protein delivery (Chapter 5, 6). A mathematical model was also developed to predict the release of histidine-tagged protein from metal-chelating ligand imprinted affinity hydrogels (Chapter 5). Finally, these two binding mechanisms were used together in a one-step photopolymerized hydrogel matrix to independently control the delivery rates of two proteins encapsulated simultaneously (Chapter 7).

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