Abstract
The separation of glycyl-leucyl-phenylalanine and its homologous was studied by reversed phase high-performance liquid chromatography. A solvatochromic interpretation (the linear solvation energy relationship and Reichardt’s ENT scale) and a non solvatochromic interpretation (Πrs factor) showed that the optimum eluent for convenient separation on a C18 stationary phase was acetonitrile/0.1 M (mol l-1) sodium citrate buffer pH 3.0, 12/88 (v/v). The retention mechanism involved appeared to be governed mainly by dipole-dipole interaction and to be influenced by the hydrogen acceptor nature of acetonitrile. In the experimental conditions, separation was only slightly influenced by the ionized status (cationic form) of the studied peptides. Finally, separation was improved by using a phenyl-bonded silica stationary phase.
