MODERN METHODS FOR DETERMINATION OF BINDING CONSTANTS:CAPILLARY ELECTROPHORESIS VS. ISOTHERMAL TITRATION CALORIMETRY
Hana Nevídalová, Zdeněk Glatz, Lenka Michalcová
Abstract
Hana Nevídalová, Zdeněk Glatz, Lenka Michalcová
Abstract
Strength of the binding between ligands (drugs) and proteins is commonly described by binding constant (Kb). These interactions have a significant effect on the biological activity, pharmacodynamics and pharmacokinetics properties of drugs. Kb can be determined by several methods. In this study capillary electrophoresis-frontal analysis (CE-FA) and isothermal titration calorimetry (ITC) are compared. Kb of systems diclofenac-HSA and lidocaine-HSA were measured by both methodologies. The results of CE-FA and ITC are comparable and can be used for investigation of other binding parameters.
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Strength of the binding between ligands (drugs) and proteins is commonly described by binding constant (Kb). These interactions have a significant effect on the biological activity, pharmacodynamics and pharmacokinetics properties of drugs. Kb can be determined by several methods. In this study capillary electrophoresis-frontal analysis (CE-FA) and isothermal titration calorimetry (ITC) are compared. Kb of systems diclofenac-HSA and lidocaine-HSA were measured by both methodologies. The results of CE-FA and ITC are comparable and can be used for investigation of other binding parameters.
Key concepts: Isothermal titration calorimetry, Capillary electrophoresis, Chemistry, Titration, Binding constant, Isothermal process, Chromatography, Electrophoresis