abstract
Although the understanding of the influence of ionic liquids (ILs) on the solubility behavior of biomolecules in aqueous solutions is relevant for the design and optimization of novel biotechnological processes, the underlying molecular-level mechanisms are not yet consensual or clearly elucidated. In order to contribute to the understanding of the molecular interactions established between amino acids and ILs in aqueous media, classical molecular dynamics (MD) simulations were performed for aqueous solutions of five amino acids with different structural characteristics (glycine, alanine, valine, isoleucine, and glutamic acid) in the presence of 1-butyl-3-methylimidazolium bis(trifluoromethyl)sulfonyl imide. The results from MD simulations enable to relate the properties of the amino acids, namely their hydrophobicity, to the type and strength of their interactions with ILs in aqueous solutions and provide an explanation for the direction and magnitude of the solubility phenomena observed in [IL + amino acid + water] systems by a mechanism governed by a balance between competitive interactions of the IL cation, IL anion, and water with the amino acids.
keywords
FORCE-FIELD; MUTUAL SOLUBILITIES; PROTEIN STABILITY; GREEN SOLVENTS; SALT-SOLUTIONS; WATER; LIPASE; HEXAFLUOROPHOSPHATE; RESOLUTION; SODIUM
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 acknowledge financial support from Fundacao para a Ciencia e a Tecnologia for Programa Ciencia 2007 and the postdoctoral grant SFRH/BPD/44926/2008 awarded to LINT. This work is partially supported by projects PEst-C/EQB/LA0020/2011 and PEst-C/CTM/LA0011/2011, financed by FEDER through COMPETE Programa Operacional Factores de Competitividade and by FCT - Fundacao para a Ciencia e a Tecnologia.