The designing of bioconjugates with enhanced activity is often limited by a lack of data on confirmation and proximities between synthetic polymer and protein molecule. Previously used methods like molecular dynamics, small-angle neutron scattering, and single-crystal structure resolving methods were unable to provide sufficient data to resolve the proximities between polymer and protein in bioconjugates. Paramagnetic Relaxation Enhancement (PRE) based <sup>19</sup>F NMR technique is a promising method to provide distance information in bioconjugates. In this work, model proteins are conjugated to the dimethyl acrylamide polymer (DMAm) through an EDC/NHS-based coupling system. The polymer backbone will be incorporated with spin labels, thus the paramagnetic center of the DMAm and NMR active nuclei in the protein will provide data about the proximities of the components in the bioconjugates. And as the catalytic activity of the enzyme can be measured by monitoring the dephosphorylation of benzoyl phosphate, it will be possible to study the effect that distance and proximities have on the function and stability of the bioconjugated protein.

Designing polymers for enhanced protein-polymer bioconjugates

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