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

Abstract

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.