Surface Plasmon Resonance (SPR) Method

Surface Plasmon Resonance (SPR) is a technique that detects mass changes resulting from intermolecular binding by flowing an analyte—a molecule exhibiting binding affinity—through a microfluidic channel toward a ligand—a molecule immobilized on a substrate. By monitoring the binding and dissociation behavior between ligands and analytes in real time, kinetic analysis can be performed. The range of evaluable molecules is diverse, including proteins (enzymes, antibodies, etc.), small molecules, macromolecules, nanoparticles, and viruses.

At U-Medico, we evaluate intermolecular interactions across multiple samples at high throughput using our SPR analysis instrument (SPR-32), equipped with a total of 32 detection sites.

Isothermal Titration Calorimetry (ITC) Method

The ITC method detects heat changes arising from intermolecular binding by titrating molecules that exhibit binding affinity for a target molecule. Unlike SPR, it does not require immobilization of molecules, enabling evaluation of binding affinity under more natural conditions. From the obtained titration curve, the binding constant (Ka), reaction binding ratio (n), enthalpy change (ΔH), and entropy change (ΔS) are determined.

At U-Medico, we have a proven track record of evaluating binding affinities for various combinations, including not only protein-protein interactions but also protein-small molecule and small molecule-small molecule interactions.

Supercentrifugation Analysis Sedimentation Velocity Method (SV-AUC)

Using SV-AUC, it is possible to analyze interactions in systems that dissociate and associate in a concentration-dependent manner. We estimate the equilibrium constant K_D for self-association and heteroassociation.

Mass Photometry

We evaluate concentration-dependent changes in association states from mass distribution and quantify dissociation constants.