Nanotemper’s Monolith MST measures binding affinities using very little sample, providing a broad range of dissociation constants (Kds) ranging from pM to mM. Because the Monolith MST uses a very small amount of sample, we can obtain Kds in a fraction of the volume and concentration as is required by isothermal titration calorimetry.
The Monolith MST is used to analyze the interactions between glycomaterials and biomolecules and is based on the detection of a temperature-induced change in fluorescence of a target as a function of the concentration of a non-fluorescent ligand. Unlike surface plasmon resonance (SPR), which immobilizes molecules often causing them to lose activity, the Monolith measures binding interaction in solution. Measuring Kds in solution allows both binding partners to freely interact in their native confirmation.
The Monolith MST is capable of characterizing interactions with many different types of glycomaterials or biomolecular samples such as glycopolymers, glycoconjugates, nanoparticles, polysaccharides, glycoproteins, small molecules, nucleic acids and vesicles. The instrument also allows us to assess competition assays and tertiary binding events, as well as the thermodynamics (ΔG, ΔH, and ΔS) from the calculated Kds.
Instrument Status: Available
The Monolith MST is a GlycoMIP-supported resource; freely available to approved users of the GlycoMIP user facility.
For access to this equipment and other GlycoMIP services, please visit the User Portal.