SPR a tool to study protein-protein interactions

Surface plasmon resonance (SPR) is the best technique to explore protein- protein interactions. In particular, SPR is important to study multiple interactions simultaneously in a proteomic approach. How does SPR work?

Protein partner, potentially interacting with your protein of interest is bound on gold coated glass slide and a solution containing your protein is flowed across the slide’s surface. When a biomolecule is attached to gold surface, so when your protein and its partner interact, the refractivity of gold changes and different angle of light can be measured. SPR was set up for the first time in 1990, and very big advances have been done for this technology. Now SPR microscopy has been proposed. The novelty of this approach consists on studying protein- protein interactions in a flat array. In this way, it’s possible to save reagents and time and increase the efficiency. Arrays of DNA, peptides, antibodies and carbohydrates are frequently reported. In certain cases aptamers substitute antibodies in order to obtain more robust interaction. The challenge of this technology is choosing the right surface and functionalise it in the best way. In an array spots have to be properly separated but the extension of surface chemistry is totally chosen by researcher and this is a great advantage.