Receptor Binding Affinity

Receptor binding affinity is the strength with which a drug, hormone, or other ligand interacts with its target receptor, helping characterize how selectively and effectively it may act. It reflects the balance between ligand-receptor association and dissociation and is commonly quantified by the equilibrium dissociation constant (Kd), with lower Kd values indicating stronger binding under defined conditions. In pharmacology, affinity measurements help compare compounds, identify potential targets, and interpret dose-response relationships alongside factors such as efficacy and receptor availability. These data support drug discovery, target validation, and the prediction of how competing ligands may influence cellular signaling and therapeutic outcomes.

Receptor Binding Affinity - Related Videos

Research

JoVE Journal - Developmental Biology

Affinity Labeling Detection of Endogenous Receptors from Zebrafish Embryos

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Cited by 1 •

2016

A novel technique for the detection of low abundance endogenous receptors present in zebrafish embryos is described. We have named it AFLIP because it consists of affinity labeling of the receptor by its ligand linked to immunoprecipitation.

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis

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Cited by 54 •

2013

Microscale thermophoresis (MST) can be widely used for determination of binding affinity without purification of the target protein from cell lysates. The protocol involves overexpression of the GFP-fused protein, cell lysis in non-denaturing conditions, and detection of MST signal in the presence of varying concentrations of the ligand.

Research

JoVE Journal - Biology
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Comparing the Affinity of GTPase-binding Proteins using Competition Assays

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Cited by 2 •

2015

This protocol compares the relative affinities of binding partners for Rho-family GTPases, including Rac1. In vivo, Rac1-binding proteins compete for a single binding interface, the conformation of which is dictated by a bound nucleotide. The nucleotide is both important and difficult to control experimentally, due to the high hydrolysis rate.

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

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Cited by 40 •

2016

The presented protocols describe two enzyme-linked immunosorbent assay (ELISA) based techniques for the rapid investigation of ligand-receptor interactions: The first assay allows the determination of dissociation constant between ligand and receptor. The second assay enables a rapid screening of blocking peptides for ligand-receptor interactions.

Research

JoVE Journal - Biochemistry
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Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

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Cited by 30 •

2017

We describe here protocols for the measurement of antibody-antigen binding affinity and kinetics using four commonly used biosensor platforms.

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