Nano-Differential Scanning Fluorimetry (nanoDSF)

Nano Differential Scanning Fluorimetry (NanoDSF) is a label-free technique for analyzing the thermal stability and folding behavior of biomolecules, including proteins, peptides, and nucleic acids. The method measures intrinsic fluorescence from aromatic amino acids, primarily tryptophan and tyrosine, as a protein undergoes thermal unfolding.

Using the Prometheus system from NanoTemper Technologies, ICE Bioscience monitors real-time changes in fluorescence intensity as a function of temperature. This supports determination of key stability parameters, including the melting temperature (T_m) and transition midpoint, under different sample conditions.

In the native folded state, tryptophan residues absorb light at 280 nm and typically emit fluorescence with a peak around 330 nm. As the protein unfolds and hydrophobic regions become exposed to the surrounding solution, the fluorescence emission profile shifts toward approximately 350 nm. Monitoring these changes in fluorescence intensity and emission wavelength as temperature increases enables determination of the protein melting temperature (T_m) and related stability behavior.

Figure. NanoDSF assay principle. Changes in the chemical environment around tryptophan residues during protein unfolding alter fluorescence intensity and emission wavelength, allowing thermal denaturation to be monitored under controlled conditions.

ICE Bioscience offers both ready-to-use NanoDSF assays and customized NanoDSF services, with the assay catalog continuously expanding.

Custom services can be adapted to specific research needs and targets, while pre-developed assays provide access to validated formats and help reduce assay-development time and resource requirements.

This combination of flexible custom solutions and ready-to-use options supports diverse stability, formulation, protein–ligand interaction, protein–protein interaction, and biomarker-validation studies across pharmaceutical and biotechnology research.