Selective Polymers For Protein Separations: Investigation of Novel Template Polymerization Techniques

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The development of cost-effective affinity separations will eventually require that expensive and labile biological affinity ligands be replaced by small chemical mimics. The Principal Investigators (PIs) have begun to develop a very promising new class of synthetic materials that are highly selective for individual proteins. These new affinity reagents are polymers which contain arrays of metal ions that bind complementary arrays of functional groups on the surface of target proteins. The novel feature that determines the selectivity of recognition of protein separations is to match the spacing of metal ions (copper) in the polymer to the spacing of metal-coordinating amino acid residues (histidine) on the protein surface. The goal of this research is to develop aqueous template polymerization monomers and techniques in order to prepare affinity polymers for protein separations and to identify the key physical and chemical properties that dictate the selectivity and strength of protein binding by the resulting materials. Three types of materials will be investigated: i) macroporous polymers, ii) thin layers of polymers that are used to coat porous beads or other surfaces, and iii) lipid vesicles. This research promises to yield a generic method for synthesizing stable and versatile selective polymers that are well-suited to cost-effective, large-scale protein purification.