Tuning protein solubilization in deep eutectic solvents (DESs) is useful for enhancing enzymatic reactions, preserving therapeutic biomolecules, and developing biomaterials, but it has only been demonstrated for a narrow range of anhydrous DESs. Here, using myoglobin as a case study, the authors show that surface modification can be used to solubilize proteins in both hydrophilic and hydrophobic DESs, with polarity and hydrogen bond capacity influencing the protein conformational state.
- Adrian Sanchez-Fernandez
- Jake H. Nicholson
- Alex P. S. Brogan
