Recent Advances in the Quantitative Determination of Protein Receptor–Ligand Interaction Kinetics

Receptor–ligand binding, which is crucial to a variety of biomedical and biochemical processes, immune responses, and signal transduction, forms the basis for many biotechnological applications. The specific binding between a receptor and a ligand is the beginning of the biological function of the receptor or ligand molecule. Therefore, a summary study of methods for quantitative determination of receptor–ligand interaction kinetics is necessary. In this review, the kinetic parameters that traditionally describe the pattern of receptor–ligand interactions are first introduced. We then summarize and analyze methods for quantitative determination of receptor–ligand interaction kinetics, including direct kinetic measurements, cytology-based measurements, computational chemistry-based measurements, and single-molecule force spectrometry technique measurements of receptor–ligand interactions. Direct measurements of the kinetics of receptor–ligand interactions are further described in methods based on surface plasmon resonance, surface-enhanced Raman spectroscopy, photoelectrochemistry, mass spectrometry binding analyses, nuclear magnetic resonance technology, and electrochemical methods. This review provides a comprehensive and accurate description of the kinetic studies of protein receptor–ligand interactions.