Unexpected elution behaviour of peptides with various reversed-phase columns

Gastrin and cholecystokinin peptides were separated by reversed-phase chromatography on conventional bristle-type and polymer-coated stationary phases. The retention of the sulphated and non-sulphated isomeric forms of both peptides is governed by the structure of the peptide, the net charge and additional polar interactions with the stationary phases. Polymer-coated phases are optimum for separations according to chain length, whereas polar interactions are required for the separation of sulphated and non-sulphated peptides of identical chain length.