CHARACTERISATION OF THE PHYSICOCHEMICAL RELATIONSHIPS OF DISPLACER IONS IN THE HIGH PERFORMANCE ION EXCHANGE CHROMATOGRAPHY OF PROTEINS

Abstract

This study explores the physicochemical relationships which underlie the interactive processes between chaotropic or kosmotropic ions, proteins and coulombic chromatographic sorbents. Variations in the chaotropic and kosmotropic properties of the displacer ion and coion permit the protein-ligand electrostatic contact area, the protein conformation, the electrostatic topology and charge distribution of the protein to be systematically probed. Moreover, these data provide guidelines relevant not only to optimisation of a particular separation task but also pertinent to new sorbent design.