NanoTemper Dianthus Molecular Screening System

Dianthus has two biophysical readouts: Spectral Shift and TRIC.
Spectral Shift leverages the power of fluorescence to detect minute variations, known as spectral
shifts, in the wavelengths of light emitted by a fluorophore that is attached to a biomolecule (the
“target”). By monitoring these spectral shifts, you can get valuable insights into the strength and
nature of the interaction between the target molecule and its ligand (binding partner).
Spectral Shift can effectively measure interactions that often prove troublesome for other
techniques. This is particularly true for interactions involving multimeric complexes, intrinsically
disordered proteins (IDPs), covalent ligands, and molecules unsuitable for biosensor
immobilization.

TRIC (Temperature-related intensity change), also known as MST (Microscale Thermophoresis),
offers a powerful biophysical technique for measuring biomolecular interactions.
TRIC is based on the temperature-dependent properties of fluorescent molecules. When
illuminated by a laser, these molecules emit light, and the intensity of this light changes with the
environment of the molecules.
To utilize TRIC for measuring biomolecular interactions, a fluorescent dye is attached to the target
molecule, e.g. a protein, and this now fluorescent target is brought into a microscopic temperature
gradient (induced by a laser). The dye fluorescence on a target molecule bound to its interaction
partner (e.g. a small molecule or another protein) experiences a different thermal effect compared
to when its present of a “free” target, thus influencing the emitted light.
The choice of dye, properties of the target and ligand molecules, and successful labeling of the
target significantly impact the sensitivity and accuracy of Spectral Shift/TRIC measurements.

Majour affinity readouts:
KD
?H
Ligand scouting
Other:
Competition Assays
Complex Inhibition Assays
Stoichiometry Assays