Nonlinear analysis of dynamic binding in affinity capillary electrophoresis demonstrated for inclusion complexes of β-cyclodextrin

The stability of the molecular host–guest inclusion complexes of β-cyclodextrin with benzoate and four different hydroxybenzoates is investigated. For the measurement of the binding constants an experimental method is devised that is based on affinity capillary electrophoresis (ACE) with indirect UV absorbance detection. We derive an explicit equation for effective mobilities in ACE experiments without violation of rigorous mass balance. This equation is employed in the nonlinear least-squares analyses of the experimental data yielding binding constants of 48±2 M−1 for benzoate, 299±38 M−1 for 2-hydroxybenzoate, 37±1 M−1 for 3-hydroxybenzoate, 228±9 M−1 for 4-hydroxybenzoate, and 895±110 M−1 in the case of 2,4-dihydroxybenzoate.