ICE Bioscience's biophysical assay platform offers a comprehensive suite of techniques that provide clients with both qualitative and quantitative insights into drug-target interactions, enabling data-driven decision-making at every stage of drug discovery. Our platform is designed to measure binding affinities, kinetics, thermodynamic properties, and protein stability, providing a deep understanding of molecular interactions and the mechanisms underlying compound efficacy.
By delivering detailed, real-time data on binding events, including interaction strength and specificity, our biophysical assays empower researchers to identify and optimize high-potential drug candidates efficiently. Whether in the early screening of large libraries or in-depth characterization of lead compounds, our platform supports clients in making accurate, high-confidence evaluations, ultimately accelerating the path to therapeutic development.
✅ Binding characterization for small molecules, PROTACs, and molecular glues.
✅ Mechanism of action studies, including identification of allosteric binders.
✅ Protein and biologic characterization: Stability, aggregation, formulation optimization, and post-translational modifications.
✅ Epitope binning and molecular weight analysis for antibody and protein variants.
| Technology | Principle | Advantages | Throughput | Data Output |
|---|---|---|---|---|
| Surface Plasmon Resonance (SPR) | SPR detects changes in the refractive index near the sensor surface. When a ligand binds to a target immobilized on the sensor, this changes the refractive index, resulting in a measurable signal. | Provides high-resolution, real-time kinetics data, enabling precise analysis of binding rates and affinity. It is ideal for lead optimization and understanding interaction dynamics. | Medium to High | Ka (association constant), Kd (dissociation constant), and binding rates (kon/koff), Rmax (maximum response). |
| Spectral Shift | Based on changes in light absorption or emission wavelength when a ligand binds to a target. These shifts are indicative of conformational changes or binding events. | Label-free and sensitive to various ligand types, making it flexible for early binding studies. It's relatively straightforward for qualitative analysis. | High | Kd (dissociation constant), qualitative analysis |
| Temperature-Related Intensity Change (TRIC) | TRIC measures temperature-dependent changes in fluorescent signal upon ligand binding. This technique is sensitive to binding-induced changes in molecular environment or size. | Works in complex media, offering high sensitivity without needing target immobilization, which preserves native protein conformation. | High | Kd (dissociation constant), real-time analysis |
| Differential Scanning Fluorimetry-Thermal Shift Assay (DSF-TSA) | DSF-TSA monitors protein unfolding by using extrinsic dyes (e.g., SYPRO Orange) that bind to hydrophobic regions exposed during denaturation, increasing fluorescence. | Cost-effective, easy to set up with commonly available equipment (e.g., qPCR machines). Suitable for high-throughput screening of protein stability. | High | Melting temperature (Tm), conformational stability (ΔTm), and insights into protein stability under varying conditions. |
| nano-Differential Scanning Fluorimetry-Thermal Shift Assay (nanoDSF-TSA) | Uses intrinsic tryptophan fluorescence to detect protein unfolding or structural changes. It measures changes in fluorescence emission as the protein's structure changes with temperature. | Measures protein stability without fluorescent dyes, providing a wide dynamic range with high precision. Higher sensitivity and small sample volume. Effective for studying thermal and chemical stability. | Medium to High | Melting temperature (Tm), conformational stability(ΔTm),and insights into protein stability under varying conditions. |
| Isothermal Titration Calorimetry (ITC) | ITC measures the heat released or absorbed during binding events, providing direct measurement of binding thermodynamics. | Directly measures binding thermodynamics, offering detailed insights into enthalpy, entropy, and stoichiometry. This allows for comprehensive analysis of interaction mechanisms. | Low | Enthalpy (ΔH), entropy (ΔS), stoichiometry (n), and Kd binding affinity. |
| Intact Mass Spectrometry (Intact-MS) | Measures the intact mass of proteins or protein complexes directly by ionizing the entire molecule and analyzing its mass-to-charge ratio (m/z) using a mass spectrometer. | Provides highly accurate molecular weight measurements for intact proteins, enabling assessment of post-translational modifications (PTMs), glycosylation, and other variants. Does not require prior digestion or fragmentation. | Low to Medium | Molecular weight, post-translational modifications (e.g., glycosylation, phosphorylation), variant profiles, and stoichiometry. |
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