receptorbindingstest

Receptorbindingstest is a general term for laboratory assays designed to quantify the interaction between a ligand (such as a hormone, drug, or neurotransmitter) and a specific receptor. The primary goals are to determine binding affinity, receptor density, and the specificity of the interaction. These tests are used across pharmacology, biochemistry, toxicology, and virology to study receptor-ligand relationships and to support drug discovery and characterisation of receptors.

Common approaches include radioligand binding assays in which a radioactively labeled ligand is used to detect binding, and non-radioactive methods such as fluorescence-based binding assays, surface plasmon resonance, fluorescence polarization, or bioluminescence resonance energy transfer. Receptors can be prepared from cell membranes, whole cells, purified receptor proteins, or immobilized on solid supports.

Typical workflow involves incubating a fixed amount of receptor with increasing concentrations of ligand to obtain a saturation curve, or using competition binding to determine affinity. After incubation, bound ligand is separated from free ligand by filtration, centrifugation, or washing. Specific binding is calculated by subtracting non-specific binding (measured in the presence of excess unlabeled ligand). Data are analyzed by nonlinear regression to yield affinity constants (Kd) and, for saturation experiments, receptor density (Bmax).

Applications include characterising receptor pharmacology, screening potential drugs, and validating targets in vaccine or antiviral research. Considerations include choosing an appropriate receptor source, maintaining physiological relevance, avoiding nonspecific binding, and handling radioactive materials safely if radioligands are used. The method’s choice depends on required sensitivity, throughput, and the receptor system studied.