Noncovalent Interactions with a Synthetic Random Heteropolymer Allow for Protein Stabilization in Nonnatural Environments

Proteins possess a vast array of functions stemming from their rich chemical diversity and hierarchical structures. For instance, enzymes exhibit catalytic properties that are more efficient than their synthetic counterparts; certain proteins can be programmed to respond to external stimuli with high selectivity and sensitivity; other proteins are critical for disease treatment. Thus, materials constructed using functional natural proteins may lead to new opportunities to address a range of scientific and technological challenges.
However, since many materials processing techniques require the use of organic solvents, proteins must be stabilized in nonnatural environments in order to develop homogenous active materials. We have developed a synthetic random heteropolymer (RHP) comprising different chemical moieties to induce multivalent interactions with the surface of proteins that are collectively strong enough to solubilize and stabilize the proteins in organic solvents. Computational simulations coupled with spectroscopic, kinetic, and light scattering experiments provide valuable insights into the nature of these interactions. Our studies show that the interactions depend highly on the physiochemical properties of the organic solvent used to dissolve the protein.