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.