Molecular Interactions & Biopharmaceuticals
MP-SPR accurately measures binding affinity and kinetics and in addition, MP-SPR offers unique capabilities and expand the applicability of the technology to a broader spectrum of samples.
Get more with MP-SPR
Surface Plasmon Resonance (SPR) has been used for measuring molecular interactions for three decades. This technology enables the evaluation of affinity and kinetics in molecular binding reactions without the need for labeling, making it a label-free technique.
MP-SPR accurately measures interactions between ligands and analytes, such as antibody-antigen or drug-target binding events. In addition, MP-SPR offers unique capabilities that enhance result reliability and expand the applicability of the technology to a broader spectrum of samples.
Key benefits of MP-SPR in molecular interaction studies
Affinity and Kinetics: Even molecules with equal affinity can exhibit vastly different kinetic profiles, underscoring the importance of kinetics as crucial selection parameters, particularly in drug discovery.
Reference channel free operation: MP-SPR’s unique PureKinetics™ feature utilizes comprehensive SPR curve measurements to provide binding information that is unaffected by solvent effects (bulk effect). Unlike traditional SPR, our technology measures bulk effects in real-time within each measurement channel, eliminating the need for a separate reference channel for bulk effect.
Compatibility with Complex Liquids: Conduct interaction measurements in diverse liquids, including complex fluids such as 100% serum, plasma and saliva (PureKinetics feature)
Multiple Ligand Capture Methods: Choose from various methods for capturing ligands, such as direct coupling, affinity capture, or membrane anchoring, depending on the nature of the attached molecule.
High Sensitivity: MP-SPR offers high sensitivity, allowing direct measurement of small molecules.
Protein research: MP-SPR is a sensitive platform to determine antibody and fragment binding on antigen
Versatile Sample Compatibility: Measure interactions with a wide range of samples including proteins, peptides, nucleotides, drug molecules, viruses, nanoparticles, living cells, and bacteria.
Capability with Lipids and Living Cells: MP-SPR instruments can accurately measure interactions involving molecules integrated into liposomes (membrane extracts) and living cells, facilitating interaction studies in natural-like environments.
Sample Conformation Analysis: Assess sample conformation, by measuring thickness of the layer.
Label-Free Detection: MP-SPR operates on a label-free detection principle, eliminating the need for labeling or modifying molecules, which preserves their natural state and simplifies assay workflows.
Discover the world of MP-SPR
Frequently Asked Questions
-
How can you measure binding kinetics?
MP-SPR dynamic flow conditions allow precise binding affinity and kinetics to be determied.
-
How can thermodynamic parameters of binding events be measured
MP-SPR can be used to determine thermodynamic parameters, such as enthalpy and entropy, by analyzing interactions kinetics at different temperatures. This helps in understanding the driving forces behind molecular interactions.
-
Does MP-SPR support screening of multiple drug candidates simultaneously?
Yes, MP-SPR allows parallel functionalization of multiple sensor channels for simultaneous screening of drug candidates. In addition, the KineticTitration function allows for the determination of kinetic constants in the sample injection series without the intermediate dissociation steps of molecules. This enchances efficiency and accelerates drug discovery workflow.
-
How can high- and low-affinity interactions be distinguished?
MP-SPR calculates binding kinetics and equilibrium constants to distinguish between strong and weak interactions. Furthermore, the PureKineticsTM feature allows for the so-called “bulk effect” removal in-situ to monitor weak interactions with small molecular weight drugs if they are dissolved in high-signal-contributing solvents such as DMSO. This is critical for identifying promising drug candidates.
-
Can QCMD monitor drug-induced conformational changes in proteins?
Yes, QCMD detects subtle dissipation and frequency shifts that correspond to conformational changes in proteins upon drug binding. This capability helps in identifying structural flexibility and stability induced by drug interactions.