Analysis of Partitioning of Organic Compounds and Proteins in Aqueous Polyethylene Glycol-sodium Sulfate Aqueous Two-phase Systems in Terms of Solute–solvent Interactions
Document Type
Article
Publication Date
2015
Keywords
Aqueous two-phase system, Partitioning, Proteins, Solute–water interactions, Solvatochromic comparison method, Solvent properties
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.chroma.2015.08.053
Abstract
Partition behavior of nine small organic compounds and six proteins was examined in poly(ethylene glycol)-8000-sodium sulfate aqueous two-phase systems containing 0.5 M osmolyte (sorbitol, sucrose, trehalose, TMAO) and poly(ethylene glycol)-10000-sodium sulfate system, all in 0.01 M sodium phosphate buffer, pH 6.8. The differences between the solvent properties of the coexisting phases (solvent dipolarity/polarizability, hydrogen bond donor acidity, and hydrogen bond acceptor basicity) were characterized with solvatochromic dyes using the solvatochromic comparison method. Differences between the electrostatic properties of the phases were determined by analysis of partitioning of sodium salts of dinitrophenylated (DNP-) amino acids with aliphatic alkyl side-chain. It was found out that the partition coefficient of all compounds examined (including proteins) may be described in terms of solute–solvent interactions. The results obtained in the study show that solute–solvent interactions of nonionic organic compounds and proteins in polyethylene glycol-sodium sulfate aqueous two-phase system differ from those in polyethylene glycol-dextran system.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Journal of Chromatography A, v. 1415, p. 1-10
Scholar Commons Citation
da Silva, Nuno R.; Ferreira, Luisa A.; Madeira, Pedro P.; Teixeira, José A.; Uversky, Vladimir N.; and Zaslavsky, Boris Y., "Analysis of Partitioning of Organic Compounds and Proteins in Aqueous Polyethylene Glycol-sodium Sulfate Aqueous Two-phase Systems in Terms of Solute–solvent Interactions" (2015). Molecular Medicine Faculty Publications. 402.
https://digitalcommons.usf.edu/mme_facpub/402