The facility offers state-of-the-art Biacore SPR instruments for label-free, real-time detection of biomolecular interactions and measurement of binding specificity, kinetic association and dissociation rates, binding affinity, and active concentration. The sensitivity and broad biomolecular sample compatibility of SPR also allows for the design of assays to assess more complex aspects of interactions such as binding thermodynamics, epitope mapping, binding mechanism resolution, and immunogen-induced antibody avidity responses in clinical sera samples.
Biacore systems are compatible with a wide range of biomolecules and can successfully measure interactions between proteins, peptides, DNA/RNA, small molecules, lipid membranes, carbohydrates, synthetic polymers, whole viruses, and whole cells. The BIA Core Facility is equipped with multiple SPR and BLI platforms and is capable of handling purified samples as well as clinically derived plasma and sera samples.
Download a poster outlining the BIA Core Facility and its capabilities here
SPR Sensorgram. A typical SPR experiment is composed of multiple analyte injection cycles using a ligand-immobilized sensor chip (1). Injection of soluble analyte complementary to the immobilized ligand results in population of the surface active sites (2) leading to saturation (3) and a corresponding increase in the SPR response. Upon completion of the injection, the bound analyte will dissociate from the surface (4) reducing the SPR response, until an injection of a regeneration buffer removes any remaining bound analyte (5) to regenerate the ligand-immobilized surface (6) in preparation for the next analyte sample. From the SPR sensorgram, the kinetics and affinity of the interaction and/or the active analyte concentration can be calculated.
- Director, S. Munir Alam, PhD
- Manager, Brian Watts, PhD