Dianthus

• High-sensitivity in-solution binding affinity screening
• Designed for challenging targets, including membrane proteins, intrinsically disordered proteins, and multimeric complexes
• Detects weak binders with affinity in the mM range
• Requires as little as 10–20 µL sample per data point
• Detects binding at target concentrations down to 250 pM
• Generates a 12-point binding curve in approximately 1 minute
• Screen up to 2,000 fragments in approximately 3 hours
• Uses two complementary readouts: Spectral Shift and TRIC
• No surface immobilization, helping reduce artifacts associated with surface-based assays
• Compatible with standard 384-well SBS-format plates
• Designed for integration with existing laboratory automation
• Exports data in CSV, XLSX, and JSON formats for downstream analysis and workflow integration

Dianthus™ is a high-sensitivity biophysical analysis platform designed for in-solution binding affinity screening and hit validation. It enables researchers to screen compound and fragment libraries while working with challenging samples that may be difficult to analyze using conventional surface-based methods.

The system combines Spectral Shift and Temperature Related Intensity Change (TRIC) to provide complementary binding information. Spectral Shift detects changes in the fluorescence emission spectrum of a labeled target to determine binding affinity, while TRIC provides an orthogonal signal to help confirm hits and identify ligand-induced effects such as aggregation.

Because measurements are performed directly in solution, Dianthus can be used with challenging targets such as membrane proteins, intrinsically disordered proteins, multimeric complexes, impure protein preparations, and low-abundance targets.

Measurement principle: In-solution binding affinity analysis
Technologies: Spectral Shift, TRIC
Sample volume: 10–20 µL per data point
Minimum target concentration: Down to 250 pM
Binding curve: 12-point curve in approximately 1 minute
Screening throughput: Up to 2,000 fragments in approximately 3 hours
Plate format: Standard 384-well SBS format
Detection: Fluorescence-based
Measurement type: Isothermal, non-destructive
Automation: Compatible with automated liquid-handling systems
Data export: CSV, XLSX, JSON
API / Integration: gRPC framework; open and FAIR APIs
Main outputs: Binding affinity, dose-response curves, hit identification
Additional analysis: Ligand-induced thermal shifts, aggregation-related effects
Slow kinetics*: kobs ≤ 1 × 10⁻² s⁻¹

*Slow Kinetics is available with the Dianthus α applications package, which extends the platform for applications such as covalent inhibitors and time-dependent binding studies.

• High-throughput affinity screening
• Fragment screening
• Hit identification
• Hit-to-lead optimization
• Drug discovery
• Small-molecule screening
• Protein–small molecule interaction studies
• Membrane protein research
• Intrinsically disordered protein (IDP) studies
• PROTAC and targeted protein degradation research
• Molecular glue research
• Covalent inhibitor characterization
• Binding site and mechanism-of-action studies
• Competitive and allosteric binding studies
• Ligand-induced protein stability analysis
• Dose-response and EC₅₀ determination