Probing with Synthetic Peptides the Interactive Properties of N-Butylphenyl and Cholesterol-10-Undecenaoate Phases Immobilised onto Open Tubular Electrochromatographic Capillaries

Abstract

This study investigates the impact of peptide primary structure and the characteristics of two different types of immobilised hydrophobic ligands on the open tubular electro-chromatographic migration behaviour of a family of related synthetic peptide analogues. The results further document the important role that mixed mode electrophoretic/chromatographic processes play in determining peptide selectivity in OTCEC systems. Procedures to fine-tune selectivity of closely related peptides in these systems have been established with buffer electrolytes of different composition in terms of the organic solvent content and different pH conditions.