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Molecular interaction analysis by SPR

Molecular interaction study with SPR (Surface Plasmon Resonance) technology

SPR systems are designed to follow in real time interactions between free-labeled biomolecules. For that, one reactant, the ligand, is immobilized on the sensor chip and the others interaction partners, named analytes, are injected at constant flow with a microfluidic circuit other the interface. The SPR principle is to follow mass changes on the surface of the sensor chip, induced by molecular complex formation and dissociation. The measured signal strength depends on both the number of ligands immobilized on the sensor chip and the mass of injected analytes. For a fixed amount of immobilized ligand, the sensitivity of detection will be even higher than the analyte has a high mass. Conversely, it is possible to detect small interaction partners only if a sufficient density of ligands (high number of receptor sites) is immobilized. The use of real-time measurement allows to provide the dynamic parameters (association and dissociation rate constants) of the interaction and to deduce the affinity.

Benefits of SPR technology :

  • qualitative and quantitative studies without molecular partners labeling
  • high sensitivity (detection of the interaction from about 1 pg of protein) and low amounts of biological material required (a few tens of micrograms)
  • measurement of the interaction in few minutes in real time
  • wide range of affinity (pM to mM)
  • nature of studied biomolecules (DNA, RNA, peptides, proteins, lipids, native biological membranes, pharmacological molecules)

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