Recent research in how natural enzymes can produce synthetic-type polymers and products provides an avenue to polymerize small molecules without organic solvents or metal catalysts. One such example is <i>Enterobacteria phage T4</i>lysozyme (T4L). Similar to other lysozymes, such as hen egg white lysozyme (HEWL), T4L can destroy bacterial cell walls through the hydrolysis of peptidoglycan residues resulting in the lysing of the bacteria. However, the research our group focuses on is a unique property that the HEWL and T4L can catalyze the polymerization of 2-ethynylpyridine (2-EP) to poly-2EP. One surprising characteristic of T4L is that it might synthesize a different product than HEWL. The polymerization of 2-EP catalyzed by T4L monitored by UV-Visible spectroscopy, shows the synthesis of a quantitatively (polymer length) or qualitatively (protein structure) different product compared to polymerization by HEWL. Also, the addition of 2-EP to <sup>15</sup>N labeled T4L produced changes in the HSQC over time associated with conformational changes of the active site. The residues perturbed with the addition of 2-EP suggests enzyme-product binding and activity. Mutations of the T4L active site, E11Q and D20A, eliminates the enzyme's ability for polymerization and/or muramidase activity, which further proves that the lytic and catalytic activity of the enzyme share a common active site. Further work to analyze the products formed by T4L and HEWL by crystallography and NMR will help determine the mechanism of the polymerization of 2-EP.

Bacteriophage lysozyme catalyzed synthesis of 2-ethynylpyridine conjugated polymer

2019 Spring National Meeting

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