High-Throughput Surface Plasmon Resonance (SPR)
For Accurate and Rapid Biologic Discovery
The early identification of a compound’s kinetics, affinity and competitive properties is crucial for making accurate decisions in the initial stages of the drug discovery process. This important phase can often be exacerbated by the requirement to investigate large compound libraries to identify molecules with the most advantageous biological properties.
Surface Plasmon Resonance Solutions
The entire Surface Plasmon Resonance (SPR) range by Sartorius has been designed with one clear focus – to allow researchers to generate the most accurate data possible in the shortest timeframe imaginable.
This is made possible by the use of patented tools exclusive to the Octet® SPR range, which include:
- OneStep® Gradient Injections: Eliminate the need for multiple analyte concentrations and significantly reduce assay development time to generate kinetics for up to 768 molecules in less than 24 hours
- OneStep® Two Component Injections: Determine accurate kinetics across multiple conditions and in the presence or absence of cofactors
- NeXtStep™ Gradient Injections: Highly accurate competition assays to examine the behavior of an analyte in the presence of a competitor molecule
Explore Octet® Surface Plasmon Resonance
SPR Promotions
Octet® SPR Solutions Feature:
- Two standard injection formats: OneStep® Injection Technology and industry standard multi-cycle kinetics (MCK)
- Eliminate the need to prepare concentration dilution series for each analyte, saving on time, reagents and plate space, and reducing potential errors in assay development
- Diffuse a single concentration of analyte into a stream of buffer to create an analyte concentration gradient of at least three orders of magnitude
- Accurate measurement of binding kinetics and affinity from a single analyte concentration
- Determine the behavior of an analyte in the presence of a competitor molecule from a single injection
- Assess multiple analytes and competitors in a single assay without the need for the competitor to be present in the running buffer
- Clearly determine full binding kinetic profiles, affinity and site-specific competition as a modulation of binding in the presence of a competitor molecule
- Generate complete kinetics and affinity for up to 768 samples in a single unattended assay
- OneStep® Injection Technology: More than 72 hours unattended run time and a unique sample layout allows for high-throughput acquisition and analysis of hundreds of samples in a single run, making the Octet® SF3 suitable for even the most high-throughput library screens
Surface Plasmon Resonance Resources
Frequently Asked Questions
Understanding Surface Plasmon Resonance
SPR sensor chips typically consist of a thin metal film, commonly gold, deposited on a glass substrate. The metal film is coated with a thin layer of a biocompatible material, often a self-assembled monolayer, to which the biomolecules of interest can be immobilized.
The sensor surface is then exposed to a liquid sample containing the analytes or target molecules. The interaction between the immobilized ligands and the analytes leads to changes in the refractive index at the surface, which can be detected and analyzed in real time.
SPR-based biosensors rely on the detection of changes in the evanescent electromagnetic field that occurs at the metal-dielectric interface when the surface plasmons are excited.
The excitation of surface plasmons is achieved by coupling a beam of polarized light, to the metal film at a specific angle known as the resonance angle. This angle is determined by the refractive index of the sample medium and the properties of the metal film.
The resonance condition is highly sensitive to changes at the metal-dielectric interface, such as the binding of a biomolecule, making SPR a powerful tool for studying biomolecular interactions.
When the incident light beam hits the metal-dielectric interface at the resonance angle, it generates an evanescent wave that extends into the sample medium. This evanescent wave interacts with the analytes in the sample, leading to changes in the refractive index near the surface. These changes can be detected as alterations in the intensity or angle of the reflected light.
A detector measures these changes, and the resulting signal is processed to obtain information about the binding events occurring on the sensor surface. By monitoring the changes in the SPR signal over time, scientists can gain valuable insights into the kinetics and affinity of biomolecular interactions of the binding process.
The rate at which the signal changes provides information about the association and dissociation of the analytes with the immobilized ligands, allowing the calculation of kinetic parameters such as association rate constants (ka or kon) and dissociation rate constants (kd or koff). The equilibrium binding affinity (KD) can also be calculated as the ratio of kd and ka or also be determined by analyzing the steady-state signal.
SPR-based biosensors enable the monitoring of dynamic processes and the analysis of fast-binding interactions. They are also highly sensitive, allowing the detection of small molecule analytes at low concentrations.
SPR technology has a wide range of applications, including drug discovery, antibody screening, protein-protein interactions, and nucleic acid interactions which provide valuable information about binding kinetics, analyte concentration, and the thermodynamics of these interactions in a label-free and real-time manner, making it an indispensable tool in many research and development settings.
Surface Plasmon Resonance is a cutting-edge technology that provides a powerful tool for studying and understanding molecular interactions. It's a key player in advancing our knowledge in biochemistry and related fields, contributing significantly to the development of new drugs and therapies.
