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Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction
Published on: February 15, 2018
Overview of the detection methods for equilibrium dissociation constant KD of drug-receptor interaction
Weina Ma1, Liu Yang1, Langchong He1
1School of Pharmacy, Xi'an Jiaotong University Health Science Center, No. 76, Yanta West Street, Xi'an, Shaanxi Province 710061, PR China.
Abstract:
Drug-receptor interaction plays an important role in a series of biological effects, such as cell proliferation, immune response, tumor metastasis, and drug delivery. Therefore, the research on drug-receptor interaction is growing rapidly. The equilibrium dissociation constant (KD) is the basic parameter to evaluate the binding property of the drug-receptor. Thus, a variety of analytical methods have been established to determine the KD values, including radioligand binding assay, surface plasmon resonance method, fluorescence energy resonance transfer method, affinity chromatography, and isothermal titration calorimetry. With the invention and innovation of new technology and analysis method, there is a deep exploration and comprehension about drug-receptor interaction. This review discusses the different methods of determining the KD values, and analyzes the applicability and the characteristic of each analytical method. Conclusively, the aim is to provide the guidance for researchers to utilize the most appropriate analytical tool to determine the KD values.
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