Surface Plasmon Resonance (SPR) is a label-free optical technique for real-time monitoring of biomolecular interactions at a sensor surface. SPR measures binding kinetics, affinity constants and concentration without the need for fluorescent or radioactive labels. It is widely used in drug discovery, protein-protein interaction studies, antibody characterization and biosensor development.
A monochromatic laser beam is directed through a prism or grating coupler to excite surface plasmons — collective oscillations of electrons — at a thin gold or silver sensor surface. At the resonance angle, light energy is transferred to surface plasmons and reflectance drops to a minimum. When molecules bind to the sensor surface, the local refractive index changes, shifting the resonance angle. By monitoring this angle shift in real time as sample flows over the sensor, binding kinetics (association rate ka, dissociation rate kd) and equilibrium affinity (KD) are determined quantitatively without any labeling.
Versatile analytical and surface characterization instruments support fundamental and applied research in molecular chemistry, reaction kinetics, colloid science, and biomolecular
Pharmaceutical R&D and manufacturing rely on surface analysis, compound characterization, and real-time interface monitoring to develop safe, effective, and consistently
Surface science and nanoscale measurement instruments support life science researchers in studying biomolecular interactions, cell adhesion, and membrane behavior with
