Biacore systems monitor molecular interactions in real time, using a noninvasive label-free technology that responds to changes in the concentration of molecules at a sensor surface as molecules bind to or dissociate from the surface. The detection principle is based on surface plasmon resonance (SPR), that is sensitive to changes in refractive index within about 150 nm from the sensor surface. To study the interaction between two binding partners, one partner is attached to the surface and the other is passed over the surface in a continuous flow of sample solution. The SPR response is directly proportional to the change in mass concentration close to the surface.
Biacore systems can be used to study interactions involving (in principle) any kind of molecule, from organic drug candidates to proteins, nucleic acids, glycoproteins and even viruses and whole cells. Since the response is a measure of the change in mass concentration, the response per molar unit of interactant is proportional to the molecular weight (smaller molecules give lower molar responses). The practical lower limit for detection of small molecules with today’s instrumentation is about 100 Da.
The detection principle does not require any of the interactants to be labeled, and measurements can be performed on complex mixtures such as cell culture supernatants or cell extracts as well as purified interactants. The identity of the interactant monitored in a complex sample matrix is determined by the interaction specificity of the partner attached to the surface. The SPR detection principle is non-invasive and works equally well on clear and colored or opaque samples.
Biacore 8K
Discover more, more efficiently
- A single solution for interaction analysis in both screening and characterization
- Screening of 2300 small-molecule fragments in a day
- High-quality kinetic characterization of 64 interactions in 4 h
- 60 h unattended runtime with queueing abilities and rapid multirun evaluations
- Confident interaction analysis of small molecules binding to complex targets such as GPCR
- Confident differentiation of high-affinity binders
Biacore T200
- A series of characteristics of intermolecular interactions, from specificity to kinetics and thermodynamics, can be analyzed by a single instrument
- Analysis software specialized for screening enables easy and fast acquisition of result
- The selection and optimization of the candidates for low molecular weight drugs and biotherapeutic drugs based on the rate of association/dissociation can be performed
- Single-cycle kinetics which eliminates the need for surface regeneration can be performed
- The quantitation of concentration is possible without using calibration curve
- The detection of immunogenicity can be achieved for non-cllinical research and clinical development
Biacore X100
- Single-cycle kinetics which eliminates the need for surface regeneration can be performed
- Solvent correction function is available for the quantitation of concentration without calibration curve (Plus package only)
- The system can be used in board range of applications from basic research to the development of diagnostiv agents and drugs.
- The user-friendly software is easy to use and provides multiple functions
- Fully automated operation using the maximum of 15 samples is possible
Biacore S200
High-sensitivity Biacore S200 increases productivity in LMW drug discovery programs and delivers reliable affinity, kinetics, or fragment-screening data from a 384-well microplate in a single day
- Outstanding sensitivity that facilitates work with difficult targets where response levels are low
- Single-concentration fragment binding data in less than 16 h.
- Affinity and kinetics determined with outstanding sensitivity for confident lead optimization
- Competition assay for validation of binders and binding site maping
- Transition-state thermodynamics for additional information about reaction mechanisms