Salt effect on partition coefficient of glycine, L-valine, and L-phenyl alanine in n-octanol-water system

The n-octanol-water partition coefficient is an important property to measure the hydrophobicity of organic compounds, which has been demonstrated to be a parameter in studying the conformation of biomolecules in aqueous solutions. The hydrophobic parameters of the amino acid side chains of peptides have been evaluated from the n-octanol-water partition coefficients of amino acids. For biological systems, electrolytes play an important role on thermodynamic properties. Numerous measurements of the partition coefficients of amino acids in the n-octanol-water system have been already made but without any salt effect. In this study, we investigated the salt effect on the n-octanol-water partition coefficients of glycine, L-valine, and L-phenyl alanine with the use of a generator column. The electrolytes used were LiCl, NaCl, and Na₂SO₄.