Receptor Affinity
Receptor Affinity - Related Videos
08:39
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.
06:01
Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
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Cited by 4 •
2019
Here, we present a protocol to screen extracellular protein microarrays for identification of novel receptor-ligand interactions in high throughput. We also describe a method to enhance detection of transient protein-protein interactions by using protein-microbead complexes.
03:07
Electron Affinity
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2020
The electron affinity (EA) is the energy change for adding an electron to a gaseous atom to form an anion (negative ion). This process can be either endothermic or exothermic, depending on the element. Many of these elements have negative values of EA, which means that energy is released when the gaseous atom accepts an electron. However, for some elements, energy is required for the atom to become negatively charged, and the value of their EA is positive. Just as with ionization energy,...
01:41
Affinity and Avidity
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2019
Overview Antibodies bind to toxins or substances on the surface of cells, bacteria, viruses, or fungi. The substance is called an antigen, and the precise binding site is the epitope. The strength of the antibody-epitope interaction is called affinity. When an antibody binds an antigen by multiple epitopes, the cumulative strength of the interaction is called avidity. The strength of the interaction influences the elicited immune response. The Adaptive Immune System Increases Efficiency by...
12:30
Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
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Cited by 56 •
2012
AVEXIS is a high throughput protein interaction assay developed to systematically screen for novel extracellular receptor-ligand pairs involved in cellular recognition processes. It is specifically designed to detect transient protein interactions that are difficult to identify using other high throughput approaches.
FAQs
At equilibrium, receptor affinity reflects the balance between ligand-receptor association and dissociation. A ligand that associates readily and dissociates less readily will generally produce a lower equilibrium dissociation constant, or Kd. Comparing Kd values therefore helps researchers rank binding strength among compounds or receptor interactions under the conditions used for measurement.
Affinity describes binding strength, whereas the magnitude of a biological response depends on additional factors. Consequently, a compound can bind strongly without producing the largest observed effect, and a weaker-binding compound may still generate a meaningful response. Pharmacologists therefore interpret affinity alongside concentration-response information rather than treating Kd as a direct measure of efficacy.
Researchers can compare a compound’s affinity across related receptor subtypes to identify interaction preferences. Substantial differences in the corresponding Kd values may indicate that binding favors one subtype over another. This comparison helps characterize selectivity during compound evaluation and can highlight receptor interactions that may contribute to intended activity or potential off-target effects.
During drug screening, affinity measurements help identify compounds that interact with a receptor and support comparison among candidates. In lead optimization, researchers can use these results to evaluate how chemical modifications affect receptor binding strength and subtype preference. The resulting comparisons help guide selection of compounds for further pharmacological investigation.
Affinity measurements provide binding information that helps place concentration-response findings in context. Comparing Kd with the concentrations associated with observed responses can support interpretation of how receptor interaction relates to pharmacological activity. Because affinity alone does not establish response magnitude, researchers use both types of information when evaluating compound behavior.
Affinity comparisons can indicate whether a compound interacts more strongly with its intended receptor than with related receptor targets. This information supports early assessment of on-target versus potential off-target interactions. In pharmacology and drug development, such comparisons help researchers interpret receptor selectivity and identify binding patterns that may warrant additional investigation.