Abstract
Log k′ w and slope values for ten β-casomorphin peptides were calculated in ten different reversed-phase liquid chromatographic systems using methanol as organic modifier. The differences between the retention behaviours of C 8, C 18 and C 30 columns were fairly small the eluent composition had a greater impact than the length of the hydrophotic ligand on the retention of peptides. A quaternary amino column showed considerably different retention characteristics. The results suggest that each substructure in the peptides makes a similar contribution to the overall retention of the peptide. The retention parameters of peptides mainly correlated with their electronic and steric characteristics. This finding emphasizes the importance of the electrostatic interactions between the free silanol groups on the surface of the reversed-phase support and the polar substructures of peptides.
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