abstract
Ion-specific effects on the aqueous solubilities of biomolecules are relevant in many areas of biochemistry and life sciences. However, a general and well-supported molecular picture of the phenomena has not yet been established. In order to contribute to the understanding of the molecular-level interactions governing the behavior of biocompounds in aqueous saline environments, classical molecular dynamics simulations were performed for aqueous solutions of four amino acids (alanine, valine, isoleucine, and 2-aminodecanoic acid), taken as model systems, in the presence of a series of inorganic salts. The MD results reported here provide support for a molecular picture of the salting-in/salting-out mechanism based on the presence/absence of interactions between the anions and the nonpolar moieties of the amino acids. These results are in good qualitative agreement with experimental solubilities and allow for a theoretical interpretation of the available data.
keywords
HYDROPHOBIC IONIC LIQUIDS; AFFECT PROTEIN STABILITY; HOFMEISTER SERIES; L-LEUCINE; MUTUAL SOLUBILITIES; AIR/WATER INTERFACE; SELF-ASSOCIATION; SODIUM-CHLORIDE; WATER-STRUCTURE; ENZYME-ACTIVITY
subject category
Chemistry
authors
Tome, LIN; Jorge, M; Gomes, JRB; Coutinho, JAP
our authors
José R. B. Gomes
Principal Researcher
Luciana Isabel Nabais Tomé
Post-doc FellowshipGroups
G4 - Renewable Materials and Circular Economy
G6 - Virtual Materials and Artificial Intelligence
acknowledgements
The authors thank Programa Ciencia 2007 and acknowledge financial support from Fundacao para a Ciencia e a Tecnologia for postdoctoral grant SFRH/BPD/44926/2008 of Luciana I. N. Tome.