Surface plasmon resonance

Advanced SPR technology for precise binding analysis

SPR is used to measure binding-mediated mass changes of immobilised targets, combining many advantages of other biophysical methods by tracking label-free molecular interactions in real time. The latest high-sensitivity instruments have no lower molecular weight limit and can quantify a large dynamic range from picomolar to weak millimolar affinities. We have extensive experience characterising protein–ligand interactions for various protein classes, including kinases, proteases, nuclear receptors, E3 ligases, GPCRs and biologics.  

Our SPR team comprises over 10 scientists and lab professionals, and our labs are equipped with a state-of-the-art platform comprising four Biacore™ T/S200 and three Biacore™ 8K/8K+ instruments. 

Binding and kinetics

Our biophysics team is highly experienced in addressing your routine questions such as binding confirmation and quantification, K_D determination and kinetic characterisation (rate constants, k_on, k_off). Additionally, we excel in deciphering modes of action, binding modes and the formation of cooperative ternary complexes (e.g., PROTAC^®s). Our SPR studies can help you elucidate interactions of small molecules with proteins, peptides, DNA and RNA, as well as interactions between biomolecules, tailored to your specific needs. Our SPR platform supports mid-scale throughput screens of fragments, focused libraries, nanobody selection and more. Instrumental in supporting our clients’ success is our in-house protein pipeline, which provides you with customised, high-quality protein samples that can be used fresh on the same day of production, helping ensure reliable and high-quality SPR data for your projects.  

SPR characterisation of the competitive binding between compounds A and B with ubiquitin for USP21. Reference: Göricke, F., et al., J Med Chem (2023)