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Extracting kinetics from affinity capillary electrophoresis (ACE) data: a new blade for the old tool.

We describe a mathematical approach that enables extraction of kinetic rate constants from thousands of studies conducted over the past two decades with affinity capillary electrophoresis (ACE). Previously, ACE has been used almost exclusively for obtaining equilibrium constants of intermolecular interactions. In this article, we prove that there exists an analytical solution of partial differential equations describing mass transfer in ACE. By using an in silico study, we demonstrate that the solution is applicable to experimental conditions that are typically used in ACE and found in most historical ACE experiments. The solution was validated by extracting rate constants from previously published ACE data and closely matching independently obtained results. Lastly, it was used to obtain previously unknown rate constants from historical ACE data. The new mathematical approach expands the applicability of ACE to a wider range of biomolecular interactions and enables both prospective and retrospective data analysis. The obtained kinetic information will be of significant practical value to the fields of pharmacology and molecular biology.