What is it about?
When a biomacromolecule interacts with a binary water–organic solvent mixture, the mixing of the three components is unequal. Organic solvent or water molecules exist preferentially in the solvation layer of the protein. This difference between the bulk solvent and solvation layer has been termed preferential solvation. We investigated water/organic solvent sorption and residual enzyme activity to monitor preferential solvation/hydration of protein macromolecules in the entire range of water content at 25oC. We applied this approach to estimate protein destabilization/stabilization due to the preferential interactions of bovine pancreatic a-chymotrypsin with water-acetone (moderate-strength H-bond acceptor) and water-DMSO (strong H-bond acceptor) mixtures.
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Why is it important?
Our data clearly demonstrate that the hydrogen bond accepting ability of organic solvents and the protein hydration level constitute key factors in determining the stability of protein–water–organic solvent systems. Facilitation of individual evaluation of the Gibbs energies of water, organic solvent, and protein constitutes one of the most important advantages of our approach.
Perspectives
Protein–water interactions play an essential role in determining the functions and stability of protein molecules. Knowledge of processes that occur upon protein hydration in the presence of organic solvents is critical in numerous biomedical and biotechnological applications, due to their utilization as biocatalysts, downstream protein processing in protein-dissolving organic solvents, and transdermal delivery of pharmaceutical proteins. For example, there are numerous advantages in employing the enzymes in the water–poor organic liquids.
Dr Vladimir A. Sirotkin
Kazanskij Privolzskij Federal'nyj Universitet
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This page is a summary of: α-chymotrypsin in water-acetone and water-dimethyl sulfoxide mixtures: Effect of preferential solvation and hydration, Proteins Structure Function and Bioinformatics, June 2017, Wiley,
DOI: 10.1002/prot.25334.
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