Surface Plasmon Resonance Spectroscopy is a technique that allows the real-time and label-free measurement of biomolecular interactions, such as
- protein-protein
- protein-DNA
- protein-polysaccharide
- enzyme-substrate or inhibitor
- antibody-antigen
- receptor-drug
- protein-virus
It can be used for a broad range of applications which include Kinetics/affinity characterization, kinetics/affinity screening, single-cycle kinetics, low molecular weight interaction analysis, fragment screening, epitope mapping, immunogenicity, concentration analysis, calibration-free concentration analysis, thermodynamics, comparability, etc.
The Biacore T200 system combines surface plasmon resonance with sensor chip technology to monitor the interaction between molecules in real time. To study the interaction between two binding partners, one interaction partner (the so-called ligand) is attached to the surface of a sensor chip and the other one (the so-called analyte) is passed over the surface in a continuous flow of sample solution. Binding of molecules to the sensor surface generates a signal response that is proportional to the mass of bound molecules and can be detected down to changes of a few pictograms or less per square millimetre on the sensor surface, corresponding to concentrations in the picomolar to nanomolar range in the sample solution. The detection principle does not require any of the interactants to be labelled, thus, biomolecules can be analysed in their native state.
The Biacore T200 system in our facility delivers high quality kinetic, affinity, concentration, specificity, selectivity, comparability and thermodynamic interaction data. It has a capacity of up to 384 samples including an autosampler that allows unattended operation. Extraordinary sensitivity makes it possible to work with a sample concentration of as little as 1 pM and up to 2 mM. The affinity range lies between 10 fM and 1 mM. The broad temperature range between 4°C and 45°C further enables the study of thermodynamic parameters.
