Analysis of amino acid-water interactions by partitioning in aqueous two-phase systems. I-Amino acids with non-polar side-chains
authors Madeira, PP; Bessa, A; Alvares-Ribeiro, L; Aires-Barros, MR; Rodrigues, AE; Zaslavsky, BY
nationality International
journal JOURNAL OF CHROMATOGRAPHY A
author keywords Amino acids; Descriptors; Hydrophobicity; Aqueous two-phase partitioning
keywords SOLVATOCHROMIC COMPARISON METHOD; PI-STAR; SCALE; PEPTIDES; HYDROPHILICITY/HYDROPHOBICITY; COEFFICIENTS; ALPHA; BETA
abstract Partition ratios of 10 L-amino acids with non-polar side chains (Gly, Ala, Val, nor-Val, Ile, Leu, nor-Leu, Phe, Trp and Pro) were measured in ten different polymer/polymer aqueous two-phase systems (ATPS) containing 0.15 M NaCl in 0.01 M phosphate buffer, pH 7.4. The solute-specific coefficients representing the solute dipole-dipole, hydrogen bonding and electrostatic interactions with aqueous environment for the compounds examined were determined by the multiple linear regression analysis using the modified linear solvation energy relationship equation. It is shown that linear combinations of these coefficients are correlated with the amino acid lipophilicity/hydrophobicity scales reported in the literature. The results obtained imply that the solute-specific coefficients may be used as solute descriptors for quantitative structure-property relationship (QSPR) analysis. (C) 2012 Elsevier B.V. All rights reserved.
publisher ELSEVIER SCIENCE BV
issn 0021-9673
year published 2013
volume 1274
beginning page 82
ending page 86
digital object identifier (doi) 10.1016/j.chroma.2012.11.080
web of science category Biochemical Research Methods; Chemistry, Analytical
subject category Biochemistry & Molecular Biology; Chemistry
unique article identifier WOS:000314443300011
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