Molecular-Level Insight of the Effect of Hofmeister Anions on the Interfacial Surface Tension of a Model Protein.

The effect of the Hofmeister anions on the precipitation of proteins is often discussed using liquid-vapor coexisting systems with the assumption that the liquid-vapor interface mimics the liquid-protein interface. Solvated proteins, however, have both hydrophobic and hydrophilic regions on their surfaces rather than just a pure hydrophobic one. Using a solvated parallel β-sheet layer consisting of both hydrophobic and positively charged hydrophilic surfaces, we investigated the adsorption of kosmotropic (SO4 2- ) and chaotropic (ClO4 - ) anions toward the protein's hydrophobic and hydrophilic surfaces via Born-Oppenheimer molecular dynamics simulations using the BLYP density functional theory. It was found that both anions prefer to reside on the hydrophilic surface. Furthermore, kosmotropic anions, like SO4 2- , enhance the interfacial surface tension of the protein and stabilize the protein, whereas, in contrast, chaotropic anions, like ClO4 - , weaken the interfacial surface tension of the protein and allow water molecules to penetrate toward the peptide bonds to form water-peptide hydrogen bonds, thus destabilizing the protein.