This system allows for the detection and monitoring of biomolecular interactions in real time, such as: protein-protein, small molecule-receptor, protein-peptide, peptide-peptide, carbohydrate-protein, lipid-protein, enzyme-substrate, antigen-antibody, DNA-protein and DNA-small molecule, among others.

This technique is often used to determine the binding specificity between two or more molecules, as well as to characterize the kinetics and affinity of the interaction. From the analysis of the data obtained, the kinetic constants of binding and equilibrium of the association/dissociation of the complex formed can be calculated. In addition, such interactions can be determined at different temperatures.

The surface plasmon resonance (SPR) technology consists of an optical phenomenon that allows for the detection of real time interactions between two or more unlabeled molecules. SPR chip-based biosensors can be used for active concentration determination and for molecular interaction characterization in terms of affinity and kinetics. To perform an SPR experiment, the ligand is immobilized onto the surface of the chip, while the analyte is injected in the system at different concentrations. When the interaction between the analyte and the ligand takes place, there is a change in the refractive index on chip surface which is measured as SPR signal or resonance units (RU) versus time. The data is represented by the system as a curve called sensorgram. The raw data is then fitted to well-defined binding models by the software, for a full characterization of the kinetic process. It is worth noting the high sensitivity of the Biacore sytem, an essential trait for measuring drug-target interactions.

This equipment has been acquired thanks to an intervention co-financiated by the European Union through the Programa Operativo del Fondo Europeo de Desarrollo Regional (FEDER) de la Comunitat Valenciana (2021-2027) (PROJECT: IDIFEDER/2021/036).

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Contact: Marta Rubio Camacho (e-mail: ; phone: 965 22 26 88).