(648i) Protein Stabilization in Non-Native Solvents with Random Copolymers

The ability to maintain the enzymatic activity of proteins out of their native aqueous medium is crucial for pharmaceutical and chemical processing industries. In foreign media such as organic and highly polar solvents, however, proteins are prone to a substantial reduction in their functionalities as their structure, solubility and conformational mobility are heavily affected. Recently, Panganiban et al. [1] demonstrated that a special case of random heteropolymers with four different monomers allow for highly effective stabilization of numerous enzymes in toluene. In this talk, we demonstrate via multiscale modeling and simulations how random copolymers with solvophobic and solvophilic groups encapsulate numerous proteins in different solvent conditions. We determine the key factors that govern the protein surface coverage of the random copolymers such as the adsorption energy, average copolymer composition and solvent selectivity. We find that the adsorbed polymer chains have considerably similar sequences, indicating that the proteins are able to select
certain copolymer sequences that best reduce their exposure to the unfavorable solvent. The results herein set the stage for computational design of random copolymers for stabilizing and delivering proteins across multiple media.

References

1. Panganiban et al. Science 2018, 359:1239-124.

*The research was supported by the Department of Energy Award No. DE-FG02-08ER46539.