Monolith

• Measures molecular binding affinity and kinetics directly in solution

• Monolith Omni combines affinity, kinetic rates, and qualitative stability in one workflow

• Uses Spectral Shift for highly sensitive detection of molecular interactions

• nanoTAK enables in-solution kinetic analysis of association and dissociation rates

• nanoLISA provides ligand-induced stability information through thermal unfolding analysis

• No surface immobilization, helping reduce mass-transport and assay-format artifacts

• Works with challenging targets, including membrane proteins, receptors, nucleic acids, molecular glues, and degraders

• Requires only a 10 µL sample for the Monolith Omni workflow

• Supports measurements under biologically relevant conditions, including detergent- and DMSO-containing buffers

• Capillary-based workflow with simple sample handling and low maintenance requirements

Monolith™ is a biophysical characterization platform for studying molecular interactions directly in solution. The system enables researchers to determine binding affinity and kinetic parameters without immobilizing either interaction partner on a sensor surface. The latest Monolith Omni extends the platform beyond affinity measurement by combining affinity, kinetic profiling, and qualitative stability analysis in a single workflow. Its solution-based approach is particularly useful for challenging targets and interactions that can be affected by surface immobilization, mass transport, molecular size differences, or assay conditions. Monolith Omni uses Spectral Shift, Nano Temperature Alteration Kinetics (nanoTAK), Nano Laser Induced Stability Analysis (nanoLISA), and Temperature Related Intensity Change (TRIC) to provide complementary information about molecular interactions.

Measurement principle: In-solution molecular interaction analysis Primary measurements: Binding affinity, kinetic rates, qualitative stability Detection technology: Spectral Shift Kinetic analysis: nanoTAK Stability analysis: nanoLISA Additional detection: TRIC Sample volume: 10 µL Measurement environment: Solution-based; no surface immobilization Kinetic range: kon up to 10⁸ M⁻¹s⁻¹; koff up to 2 s⁻¹ Temperature range for nanoLISA: up to 95°C Sample format: Capillary-based workflow Data: Affinity, association rate, dissociation rate, ligand-induced stability information Software: Monolith control and analysis software

• Drug discovery and development

• Binding affinity measurement

• Kinetic profiling

• Antibody characterization

• Protein–protein interaction studies

• Protein–small molecule interactions

• Small-molecule and fragment screening

• Membrane protein research

• Receptor–ligand interaction studies

• Nucleic acid interactions

• Molecular glue research

• Targeted protein degradation (TPD) / degrader studies

• PROTAC research

• Intrinsically disordered protein (IDP) studies

• Biophysical characterization of challenging targets

• Ligand-induced protein stability studies