Dual protein delivery from monophasic hydrogels prepared in situ

PMSE 564

Andrew T. Metters, metters@clemson.edu, Department of Chemical and Biomolecular Engineering, Clemson University, 127 Earle Hall, Clemson, SC 29634-0909 and Chien-Chi Lin, chiencl@clemson.edu, Department of Bioengineering, Clemson University, 401 Rhodes Hall, Clemson University, Clemson, SC 29634.
Monophasic affinity hydrogels which overcome the limitations of current heterogeneous polymeric formulations for dual protein delivery have been prepared. Hydrogel formation and multi-protein encapsulation in aqueous solution are achieved in a single, highly efficient fabrication step. Two model proteins, lysozyme and hexahistidine-tagged green fluorescent protein (his-GFP), were uniformly encapsulated within hydrogels composed of polyethylene glycol (PEG) and metal-ion affinity ligand – methacrylated iminodiacetic acid (GMIDA). Using this novel system, the release rate of any his-tagged protein can be adjusted independently without changing the release rate of a second, non-tagged protein. This affinity hydrogel system remains highly hydrophilic and is considered to be a promising technique in the field of controlled release and tissue engineering.