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Protein separation by monolithic capillary electrochromatography.

Dirk Bandilla1, Cameron D Skinner

  • 1Department of Chemistry and Biochemistry, Concordia University, 1455 de Maisonneuve Boulevard Ouest, Montréal, PQ Canada, H3G 1M8.

Journal of Chromatography. A
|August 22, 2003
PubMed
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This study demonstrates capillary electrochromatography using a C4 monolithic stationary phase for protein separation. While offering higher resolution than capillary zone electrophoresis, reproducibility was improved with a sodium dodecyl sulfate rinse.

Area of Science:

  • Analytical Chemistry
  • Separation Science

Background:

  • Capillary electrochromatography (CEC) combines electroosmotic flow and chromatographic principles.
  • Monolithic stationary phases offer advantages in flow resistance and surface area.
  • C4 functionality is explored for hydrophobic interaction-based protein separations.

Purpose of the Study:

  • To develop and evaluate a C4 monolithic stationary phase for capillary electrochromatography.
  • To assess the separation efficiency, resolution, and reproducibility of the CEC system for model proteins.
  • To investigate the influence of mobile phase composition and velocity on protein separation.

Main Methods:

  • Fabrication of a C4 monolithic stationary phase in UV-transparent capillaries via photopolymerization.
  • Separation of model proteins using capillary electrochromatography.

Related Experiment Videos

  • Evaluation of separation efficiency (theoretical plates) and resolution.
  • Assessment of inter- and intra-column reproducibility with and without a sodium dodecyl sulfate (SDS) rinsing procedure.
  • Investigation of mobile phase velocity and injection time effects on separation performance.
  • Analysis of protein capacity factors in relation to organic solvent percentage in the mobile phase.

    • Main Results:

    • The C4 monolithic CEC system achieved theoretical plate numbers between 11,000 and 33,000.
    • Separation efficiency was lower than capillary zone electrophoresis (18,000–66,000 plates) but resolution was higher due to the dual separation mechanisms.
    • Intra-column reproducibility was significantly improved by a mobile phase rinse containing 0.05% SDS.
    • Plate heights were largely independent of mobile phase velocities above 0.5 mm/s.
    • Protein capacity factors increased with higher organic solvent percentages in the mobile phase.

    Conclusions:

    • C4 monolithic capillary electrochromatography provides a viable method for protein separation with enhanced resolution.
    • Optimization of rinsing procedures is crucial for improving reproducibility in monolithic CEC systems.
    • The developed CEC method allows for high-velocity operation without compromising separation efficiency.
    • Further studies can explore the application of this C4 monolithic CEC for complex protein mixture analysis.