SPR Assays (or Surface Plasmon Resonance) measure biomolecular intonations, including small molecules/protein and protein/protein interactions. Reaction Biology is equipped with the state of the art Biacore 8K instrument with high throughput capability and extreme detection sensitivity.
With the new Biacore 8K SPR platform, RBC provides:
- High throughput fragment library screening
- Kinetics and affinity determination
- Binding site mapping and competition analysis
- Specificity determination
- Antibody characterization
today to discuss using our SPR assays in your project!
Related To SPR Assays
Scientists are increasingly moving to SPR to accelerate their drug discovery efforts. Some of the ways SPR can do this:
- 1. Provide useful lead optimization earlier in the process. With SPR’s low data cost, affinity and kinetics information on hit compounds can be ordered earlier in the process. While biochemical inhibition data can determine a hit, affinity and residence time data can give more information as to the pharmaceutical properties of a compound. By applying this analysis during early synthesis rounds, the SPR user avoids late failures of lead candidates. In particular there has been increased focus on binding kinetic studies during lead optimization, especially residence time. Optimization of this parameter can improve drug efficacy in vivo as well as reduce off-target mediated toxicity, hence, improving drug safety and tolerability.
- 2.Enable fragment screening. SPR can measure weak binding with very low molecular weight inhibitors (M 80-300), low millimolar affinity levels, and very fast on and off rates. Our platform allows us to screen a 2300 fragment library in a day, with automatic detection of atypical binding behavior. This enables fragment screening as a replacement for the typical small molecule screen of larger libraries.
- 3.Interactions involving challenging targets. Not all targets have a useful biochemical assay fully validated. Even if a biochemical assay is not complete, binding data can be determined between any ligand and binder. Some target environments such as hybridoma supernatants, cell membranes, or serum samples have only a crude matrix to analyze. SPR can deal with native preparations and low activity without jeopardizing results.
- 4. Low immobilization maximizes accurate results. Low immobilization levels generally give fewer secondary interactions and increase the proportion of target accessible for binding. SPR enables measurement of very fast on-rates that allows differentiation between rapid binders. This is an important feature when studying biological processes limited by bioavailability.
- 5. A lower cost alternative. Accurate interaction analysis of LMW fragments binding to targets with low activity levels also provides valuable insights to the interaction process while offering a higher throughput alternative to X-ray crystallography and NMR for secondary screens and characterization of selected hits.