The individual enantiomers of a racemic drug usually exhibit specific therapeutic efficacy. In order to achieve optimal
therapeutic treatment, an enantioselective analytical method is needed for quality control. Capillary electrophoresis
is an analytical method which shows high efficiency in enantiomeric separation. In this study, the enantioselectivity
of two calcium channel blockers was investigated using chiral macromolecule as a selector in the background
electrolyte of the capillary electrophoresis system. Polysaccharide-based and protein-based selectors were
employed separately, each at different concentrations and conditions (e.g., pH value and applied voltage) to achieve
baseline separation. Furthermore, the interaction of each enantiomer with human serum albumin as the most
abundant protein in the biological system was studied. Mobility-shift affinity capillary electrophoresis was applied to
perform the enantiomeric separation and the determination of binding constant. The apparent binding constant of
each enantiomer was measured by nonlinear regression analysis. The R- and S- enantiomers of each drug model
showed different binding constant value
