Kinetic Study of Chiral Intermolecular Interactions by Moment Analysis Based on Affinity Capillary Electrophoresis

Capillary electrophoresis
is a method for analyzing intermolecular
interactions that does not require immobilization of molecules to
a solid surface or introduction of a luminescent moiety. Recently,
an advanced method, moment analysis based on affinity capillary electrophoresis
(MA-ACE), was developed. This method can determine not only the equilibrium
constant but also the rate constants of an intermolecular interaction.
Through MA-ACE, it became possible to theoretically predict an increase
in the variance of an observed peak caused by intermolecular interaction.
In this study, we confirm the prediction and determine the kinetic
constants by using MA-ACE to analyze an intermolecular interaction
between cyclodextrin and phenoxypropionic acid. A numerical calculation
is performed to confirm that the derived rate constants by MA-ACE
are appropriate.