Chiral separation of DL‐peptides and enantioselective interactions between teicoplanin and D‐peptides in capillary electrophoresis

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Abstract
Teicoplanin has been evaluated as a selector for enantioseparation of di‐ and tripeptide derivatives in capillary electrophoresis. Separation variables such as type of buffer, pH, concentrations of teicoplanin and organic modifier were examined. Optimal separation conditions were obtained by means of factorial design experiments. The effects of teicoplanin concentrations below and above its critical micellar concentration (CMC) and of acetonitrile (ACN) on the separation were demonstrated. The use of a high concentration of ACN resulted not only in increased selectivity, but also in improved separation efficiency. Electroosmotic flow was observed to be largely independent of the concentrations of teicoplanin under the optimized conditions. Good repeatability of migration times was obtained. The interactions between teicoplanin and D and L peptides were studied, and it was found that, for some peptides, teicoplanin exhibited enantioselective interaction only with the D‐form. Somewhat lower separation efficiencies were thus observed for the strongest interacting (D‐form) peptides. Chiral separation of 15 DL‐peptide derivatives was achieved in less than 10 min.

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