Competitive Effects of Anions on Protein Solvation by Aqueous Ionic Liquids.

ABSTRACT: The present study utilizes molecular dynamics simulations to examine how different anions compete for protein solvation in aqueous solutions of ionic liquids (ILs). Ubiquitin is used as model protein and studied in IL mixtures sharing the same cation, 1-ethyl-3-methylimidazolium (EMIM), and two different anions in the same solution, from combinations of dicyanamide (DCA), chloride (Cl), nitrate (NO₃), and tetrafluoroborate (BF₄). Our findings reveal that specific interactions between anions and the protein are paramount in IL solvation, but that combinations of anions are not additive. For example, DCA exhibits a remarkable ability to form hydrogen bonds with the protein, resulting in a significantly stronger preferential binding to the protein than other anions. Howe

SUBMITTER: Piccoli V 

PROVIDER: S-EPMC11331513 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature