Overview
Nanotemper’s Monolith MST measures binding affinities using very small sample volumes, providing access to a broad range of dissociation constants (Kd) spanning picomolar to millimolar values. Because the Monolith MST requires minimal sample volume and concentration, reliable Kd values can be obtained using a fraction of the material typically required for techniques such as isothermal titration calorimetry.
Description
The Monolith MST is used to analyze interactions between glycomaterials and biomolecules by detecting temperature‑induced changes in fluorescence of a target molecule as a function of the concentration of a non‑fluorescent ligand. Unlike surface plasmon resonance (SPR), which requires immobilization of one binding partner and can alter molecular activity, the Monolith MST measures binding interactions entirely in solution.
Measuring Kd values in solution allows both binding partners to freely interact in their native conformations, providing biologically relevant interaction data.
Applications
The Monolith MST supports characterization of interactions involving a wide range of glycomaterials and biomolecular samples, including:
- Glycopolymers and glycoconjugates
- Nanoparticles and polysaccharides
- Glycoproteins and small molecules
- Nucleic acids and vesicles
The instrument also enables assessment of competition assays and tertiary binding events, as well as thermodynamic parameters (ΔG, ΔH, and ΔS) derived from calculated Kd values.
Instrument Status:
Available
User Access:
The Monolith MST is a GlycoMIP‑supported resource and is freely available to approved users of the GlycoMIP user facility.
For access to this equipment and other GlycoMIP services, please visit the User Portal.