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A ligand binding assay (LBA) is an assay, or an analytic procedure, which relies on the binding of ligand molecules to receptors, antibodies or other macromolecules. [1] A detection method is used to determine the presence and amount of the ligand-receptor complexes formed, and this is usually determined electrochemically or through a fluorescence detection method. [2]
In DNA-ligand binding studies, the ligand can be a small molecule, ion, [1] or protein [2] which binds to the DNA double helix. The relationship between ligand and binding partner is a function of charge, hydrophobicity, and molecular structure. Binding occurs by intermolecular forces, such as ionic bonds, hydrogen bonds and Van der Waals forces.
Rotating cell‑based ligand binding assay using radioactivity or fluorescence, is a recent method that measures molecular interactions in living cells in real-time. This method allows the characterization of the binding mechanism, as well as K d, k on and k off. This principle is being applied in several studies, mainly with protein ligands ...
The binding of a ligand to a macromolecule is often enhanced if there are already other ligands present on the same macromolecule (this is known as cooperative binding). The Hill equation is useful for determining the degree of cooperativity of the ligand(s) binding to the enzyme or receptor.
In biochemistry, receptor–ligand kinetics is a branch of chemical kinetics in which the kinetic species are defined by different non-covalent bindings and/or conformations of the molecules involved, which are denoted as receptor(s) and ligand(s). Receptor–ligand binding kinetics also involves the on- and off-rates of binding.
Historically, the ligand binding assay was used to determine ER activity. This method was limited because large quantities of fresh tissue were needed for each assay. IHC can be performed on fixed tissue and needle biopsies, [2] and is more accurate in assessing ER status of a tumor. [3]
Molecular recognition plays an important role in biological systems and is observed in between receptor-ligand, [16] [17] antigen-antibody, DNA-protein, sugar-lectin, RNA-ribosome, etc. An important example of molecular recognition is the antibiotic vancomycin that selectively binds with the peptides with terminal D-alanyl-D-alanine in ...
Saturation binding measures the specific binding of a radioligand at varying concentrations while at equilibrium. Through this method, the number of receptors can be determined as well as affinity of the ligand to these receptors. Saturation binding experiments are often called "Scatchard experiments" as they can be graphed as a Scatchard plot ...