Analysis of partitioning of organic compounds and proteins in aqueous polyethylene glycol-sodium sulfate aqueous two-phase systems in terms of solute-solvent interactions

J Chromatogr A. 2015 Oct 9:1415:1-10. doi: 10.1016/j.chroma.2015.08.053. Epub 2015 Aug 28.

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 0.5M osmolyte (sorbitol, sucrose, trehalose, TMAO) and poly(ethylene glycol)-10000-sodium sulfate system, all in 0.01M 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.

Keywords: Aqueous two-phase system; Partitioning; Proteins; Solute–water interactions; Solvatochromic comparison method; Solvent properties.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry
  • Dextrans / chemistry
  • Hydrogen Bonding
  • Polyethylene Glycols / chemistry*
  • Proteins / chemistry*
  • Solvents
  • Static Electricity
  • Sulfates
  • Water

Substances

  • Amino Acids
  • Dextrans
  • Proteins
  • Solvents
  • Sulfates
  • Water
  • sodium sulfate
  • Polyethylene Glycols
  • polyethylene glycol 8000