Lopez-Polo, JJLopez-PoloArratia-Perez, RamiroRamiroArratia-PerezCantero-Lopez, PlinioPlinioCantero-LopezPaez-Hernandez, DayanDayanPaez-HernandezSilvestre Paez-Meza, ManuelManuelSilvestre Paez-MezaYanez-Osses, OsvaldoOsvaldoYanez-Osses2025-04-232025-04-23201710.1016/j.cplett.2017.08.067https://sic.vriic.usach.cl/entities/publication/6ed12ee4-b1e8-4005-af14-3290161dfd4fThe molecular interactions that promote the stability of proteins and amino acids in saline solutions is a central topic of molecular biophysics. However, a well-supported molecular picture of the phenomena has not been established yet. In this paper, we studied as model system the mix between DL-Alanine in aqueous solutions of STP (Na2S2O3·5H2O) at different temperatures, from volumetric and viscometric properties. The thermophysical properties obtained indicate the presence of a strong preferential solvation, structure-making action and a possible salt in effect. Quantum chemical calculations and molecular dynamic (MD) simulations provide a new insight to support these arguments. © 2017 Elsevier B.V.en-UShttps://doi.org/10.1016/j.cplett.2017.08.067