Our MST-TRIC service combines the principles of MicroScale Thermophoresis (MST) and Temperature-Related Intensity Change (TRIC) to characterize molecular interactions in solution. This approach measures binding at equilibrium and supports the determination of dissociation constants (Kd) under physiologically relevant conditions.
By monitoring ligand-induced changes in fluorescence intensity during a brief, localized temperature shift, MST-TRIC provides a sensitive and flexible method for analyzing interactions between proteins, small molecules, fragments, and multi-component complexes.
MST-TRIC measures changes in fluorescence intensity after a brief, localized infrared-laser heating step. When a fluorescently labeled molecule binds to a ligand, the local chemical environment around the fluorophore changes. These binding-dependent effects become more pronounced during the temperature shift, enabling sensitive detection of molecular interactions.
The assay is performed in solution and does not require immobilization or microfluidic handling, helping preserve native molecular behavior during affinity measurements.
Nanotemper Dianthus and assay principle. The MST-TRIC assay is based on the principle that when a target molecule interacts with a ligand, the chemical environment around the fluorophore attached to the target molecule changes. This interaction causes a temperature-related shift in fluorescence intensity. During detection, an infrared laser briefly heats the measurement site, and the resulting temperature-induced fluorescence fluctuations are monitored to identify and quantify binding events.
Highly active, in-house produced proteins support a broad range of biophysical assay requirements.
Supports single-dose screening of small molecules and fragments, affinity analysis for hit validation and hit-to-lead studies, classification after high-throughput screening, structure–activity relationship studies, characterization of binary and ternary degrader complexes, and protein–protein interaction or signaling studies.
The Dianthus system enables sensitive detection of spectral and fluorescence-intensity changes, supporting affinity measurements that can reach the picomolar range.
The platform can complete 384-well microplate detection in approximately 73 minutes, supporting efficient screening and affinity characterization.
The microplate-based, microfluidic-free format operates entirely in solution and is independent of molecular-weight variation, making it suitable for challenging screening projects.
Fluorescently label the target molecule.
Mix the labeled molecule with a gradient dilution of the ligand.
Place the sample in the instrument and briefly heat the detection site with an infrared laser.
Plot normalized fluorescence intensity, Fnorm, against ligand concentration to calculate the binding affinity constant, Kd.
BRD2 binds acetylated lysine residues and contributes to chromatin remodeling, transcriptional regulation, cell proliferation, and apoptosis. These functions make BRD2 a relevant target for discovery-stage research.
A library of 324 fragments was screened against BRD2 (BD2) using MST-TRIC. Candidate binders identified in the primary screen were subsequently evaluated by affinity measurement to confirm their interaction with the target.
Figure. MST-TRIC supports BRD2 (BD2) drug discovery. A. Single-dose screening using MST-TRIC, with identified hits shown in light purple. B. Distribution of binders after the primary screen; binders accounted for 8% of the screened fragment library. C. MST-TRIC binding-affinity measurements confirmed the interaction of a representative hit with BRD2 (BD2).
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