Biophysical Assays: Overview

Biophysical Assay Platform

ICE Bioscience’s biophysical assay platform provides qualitative and quantitative insight into drug-target interactions, supporting data-driven decisions throughout drug discovery. Our technologies measure binding affinity, kinetics, thermodynamic properties, and protein stability to clarify molecular interactions and compound mechanism.

From early library screening to in-depth lead characterization, our platform delivers real-time binding data on interaction strength and specificity to support high-confidence candidate evaluation and therapeutic development.

Applications

Molecular Interaction Questions Addressed

01 Binding Characterization Characterize binding for small molecules, PROTACs, and molecular glues.	02 Mechanism of Action Studies Support mechanism-of-action studies, including identification of allosteric binders.
03 Protein and Biologic Characterization Assess stability, aggregation, formulation optimization, and post-translational modifications.	04 Antibody and Protein Variant Analysis Support epitope binning and molecular-weight analysis for antibodies and protein variants.

Technology Comparison

Technology	Principle	Advantages	Throughput	Data Output
Surface Plasmon Resonance (SPR) ↗	Detects refractive-index changes near a sensor surface when a ligand binds an immobilized target.	High-resolution, real-time kinetic data for precise binding-rate and affinity analysis; suitable for lead optimization and interaction-dynamics studies.	Medium to High	K_a, K_d, k_on/k_off, R_max
Spectral Shift ↗	Measures changes in light absorption or emission wavelength when a ligand binds a target.	Label-free and sensitive to multiple ligand types; flexible for early binding studies and straightforward qualitative analysis.	High	K_d, qualitative analysis
Temperature-Related Intensity Change (TRIC) ↗	Measures temperature-dependent fluorescent-signal changes following ligand binding.	Works in complex media with high sensitivity and without target immobilization, helping preserve native protein conformation.	High	K_d, real-time analysis
Differential Scanning Fluorimetry-Thermal Shift Assay (DSF-TSA) ↗	Monitors protein unfolding with extrinsic dyes that bind hydrophobic regions exposed during denaturation.	Cost-effective and easy to set up on commonly available equipment; suitable for high-throughput protein-stability screening.	High	T_m, ΔT_m, conformational stability
nano-Differential Scanning Fluorimetry-Thermal Shift Assay (nanoDSF-TSA) ↗	Uses intrinsic tryptophan fluorescence to detect protein unfolding or structural changes with temperature.	Dye-free stability measurement with wide dynamic range, high precision, high sensitivity, and low sample-volume requirements.	Medium to High	T_m, ΔT_m, conformational stability
Isothermal Titration Calorimetry (ITC) ↗	Measures heat released or absorbed during binding events for direct thermodynamic measurement.	Directly measures binding thermodynamics, providing detailed insight into enthalpy, entropy, stoichiometry, and interaction mechanisms.	Low	ΔH, ΔS, n, K_d
Intact Mass Spectrometry (Intact-MS) ↗	Measures intact protein or protein-complex mass directly through mass-to-charge ratio analysis.	Accurate molecular-weight measurement for intact proteins, post-translational modifications, glycosylation, and other variants without prior digestion or fragmentation.	Low to Medium	Molecular weight, PTMs, variant profiles, stoichiometry

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Biophysical Assays: Overview

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