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Moment analysis for reaction kinetics of intermolecular interactions
1Department of Chemistry, Faculty of Science, Rikkyo University, Toshima-ku, Tokyo, Japan.
Electrophoresis
|August 30, 2018
Summary
This study introduces moment equations based on relativity to analyze elution peaks from Affinity Chromatography (ACE). These equations accurately determine association (ka) and dissociation (kd) rate constants for molecular interactions.
Area of Science:
- Biophysical Chemistry
- Analytical Chemistry
- Chemical Kinetics
Background:
- Affinity Chromatography (ACE) is crucial for studying molecular interactions.
- Analyzing ACE elution peak profiles is key to determining binding kinetics.
- Existing methods may have limitations in extracting kinetic information.
Purpose of the Study:
- To develop novel moment equations for analyzing ACE elution peak profiles.
- To analytically determine association (ka) and dissociation (kd) rate constants.
- To investigate the influence of mass transfer and kinetics on ACE peaks.
Main Methods:
- Developed moment equations based on the principle of relativity.
- Transformed basic ACE equations between Galilean coordinate systems (S and S').
- Derived moment equations in the time domain from Laplace domain solutions.
- Applied inverse Galilean transformation to obtain moment equations in the original system.
Main Results:
- Successfully determined ka and kd values from published ACE data.
- Demonstrated the effectiveness of moment equations in extracting affinity kinetics.
- Analyzed the impact of mass transfer and reaction kinetics on ACE peak profiles.
Conclusions:
- The developed moment equations provide an effective analytical tool for ACE data.
- This method enhances the understanding of intermolecular interaction kinetics.
- The approach offers insights into factors influencing elution peak shapes in ACE.
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