Abstract

Polycationic protegrin analogs were studied by reverse-phase high performance liquid chromatography (RP-HPLC) and capillary zone electrophoresis (CZE). A total of thirty-three peptides were tested to evaluate their separations by HPLC and CZE. The peptides included single amino acid substitutions (D and L isomers), truncated amino- and carboxy-termini, cyclic and all D-amino acid analogs. The separation by CZE was achieved due to charge/mass difference of these peptides. The peptide analog mobility fit the Offord equation. Separation between peptides having the same charge/mass also occurred with some single D-amino acid substituted analogs. A completely different separation profile was obtained by RP-HPLC RP-HPLC exhibited better separation of the single D-amino acid substituted analogs, while CZE showed better separation of the truncated analogs. The use of HPLC and CZE provides an orthogonal separation tool for protegrin peptides

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