2015Unpublished venueRequires access

Comparison of capillary electrophoresis and isothermal titration calorimetry for determination of the binding constant

Lenka Michalcová, Hana Nevídalová, Zdeněk Glatz

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Abstract

The binding constant is commonly used to describe the strength of binding between ligands (drugs) and protein. The strength of the interaction has a significant effect on the biological activity of the drug, and knowledge of the nature and extent of drug-protein binding can help us to understand the pharmacokinetics and pharmacodynamics of a drug. The binding constant may be determined by various methods. The main objective of the study was to compare the results of capillary electrophoresis and isotermal titration calorimetry.

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What this paper is about

The binding constant is commonly used to describe the strength of binding between ligands (drugs) and protein. The strength of the interaction has a significant effect on the biological activity of the drug, and knowledge of the nature and extent of drug-protein binding can help us to understand the pharmacokinetics and pharmacodynamics of a drug. The binding constant may be determined by various methods. The main objective of the study was to compare the results of capillary electrophoresis and isotermal titration calorimetry.

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Available abstract

The binding constant is commonly used to describe the strength of binding between ligands (drugs) and protein. The strength of the interaction has a significant effect on the biological activity of the drug, and knowledge of the nature and extent of drug-protein binding can help us to understand the pharmacokinetics and pharmacodynamics of a drug. The binding constant may be determined by various methods. The main objective of the study was to compare the results of capillary electrophoresis and isotermal titration calorimetry.

Key concepts: Isothermal titration calorimetry, Capillary electrophoresis, Binding constant, Titration, Chemistry, Constant (computer programming), Chromatography, Plasma protein binding

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