Our research group aims to synthesize enzyme-like catalysts by mimicking the structural aspects of a biological enzyme’s active site to achieve the selectivity, reactivity, and specificity of metal-containing enzymes such as dopamine β-monooxygenase. Our design combines a transition metal complex with a synthetic polymer-based scaffold to mimic both the primary and secondary coordination spheres of an enzyme. We hypothesize that the addition of a polymer as a mimic of the secondary coordination sphere will provide a microenvironment similar to that of an enzyme by producing steric effects and non-covalent interactions between the polymer and substrates bound to the metal center, improving the reactivity and tunability of our “metallopolymer.” We have reproduced the synthesis of two literature-based copper complexes and have modified each of the ligand precursors to include two vinyl moieties. These moieties allow our ligand precursors to be directly incorporated into a polymer scaffold via copolymerization. Currently, we are focusing on the copolymerization of our vinylated ligand precursors with commercial monomers using reversible addition-fragmentation chain transfer (RAFT) polymerization to synthesize star polymer scaffolds as well as the metalation of the resulting polymer scaffolds to yield our desired copper-based metallopolymer. The catalytic oxidation activity of these metallopolymers will be tested and compared to the non-polymer-bound analogs we synthesized as benchmarks. These studies will allow us to determine how the addition of the polymer microenvironment changes reactivity and selectivity in these oxidation reactions.

Towards enabling enzyme-like catalysis through polymer-bound copper complexes

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