The Molecular Interactions Platform is equipped with a Biacore T200 (new generation) and a Biacore 3000.

This technology uses surface plasmon resonance (SPR) for the real-time characterisation of interactions between a molecule immobilised on the surface of a sensorchip (ligand molecule) and a molecule in solution (analyte molecule) infused at a constant rate via a microfluidic system.
Monitoring variations in the SPR signal as a function of time (sensorgram) with several analyte concentrations enables kinetic determination of the association and dissociation rates and deduction of the affinity constant.
As its name indicates, the BIA technology (Biomolecular Interaction Analysis) can measure the dynamic parameters of interactions between biomolecules (non-labelled) such as:
– Peptides-proteins/proteins
– DNA-RNA/proteins
– Sugars/proteins
– Membrane vesicles/ligands
– Liposomes/proteins
– Synthetic molecules/biomolecules

Classic applications:
– Interaction dynamics: measurement of association (ka), dissociation (kd) and affinity (KD) constants.
– Measurement of molecular concentrations.
– Mapping of epitopes (antibodies) and binding sites.
– Studies of interactions between numerous molecules.

Functional proteomics:
– Micro-purification of proteins for enzymatic digestion and identification and/or sequencing under mass spectrometry (coupled BIA/MS).
– Screening of the ligands of orphan receptors.
– Determination of the level of expression of proteins of interest under different cultivation conditions or treatments.