Our group discovered a novel enzymatic activity by placing horseradish peroxidase (HRP) in presence of ARGET ATRP reagents for the polymerization of N-isopropylacrylamide. 16 Reactions without one of the reagent, i.e. reducing agent, catalyst or initiator, yielded no polymers. Analysis of the polymers formed via COSY 1H NMR confirmed the presence of ATRP initiator in the polymer chains. Neutron scattering experiments revealed that 67% of end-chains were bromine terminated pointing toward an ATRP mechanism. The reaction was highly dependent on pH and optimal condition at pH 6 yielded polymeric chains with dispersity as low as 1.44 were synthesized. As none of the other reagents are affected by pH, this constituted the first evidence of the …show more content…
The reasoning is that the active center alone is not sensitive to its environment and reaction conditions as the enzyme. Therefore, using solely the active center would make it a more robust catalyst. 3. Enzyme mimetic catalyzed ATRP The first study of this type of catalyst was carried out by Simakova et al.22 They started using hemin which is like the iron surrounded by porphyrin found in HRP, hemoglobin or catalase to polymerize PEGA. However due to its low halidophilicity, low solubility in water and possible incorporation in polymer chains due to its double bonds, controlled polymerization could not be achieved. Addition of KBr to reinforce deactivation but also to fasten initiation permitted to obtain polymer with narrow dispersity. This was considerably enhanced upon PEGylation of the catalyst to increase its water-solubility. Concurrently, Yamashita et al.23 reported the polymerization of NIPAM also using hemin as catalyst. However, they obtained quite broad dispersity confirming that hemin itself does not suffice to obtain control over the reaction. However, they could show that polymer were formed via an ATRP-like