Tailored NMR Projects for Industry
NMR is a highly versatile technique that can support a range of drug-discovery activities. Building on our many years of experience, we offer tailor-made NMR solutions covering the entire NMR workflow—including protein production, assay design and development, screening, and data evaluation. We also have experience in setting up NMR-based mode-of-action studies and enzymatic assays.
Our NMR services include the following:
- Protein production for NMR: Streamlined and tailored solutions to produce isotopically labeled proteins required for NMR experiments (15N/13C/2H). Further details: protein sciences.
- Protein-observed NMR: Robust and information-rich NMR methods to validate and characterize the binding of a compound to its target. Binding site identification can be performed for targets whose NMR signals have been assigned to their respective amino acids. Further characterization may include determination of ligand binding affinity, protein folding and dynamics, and general protein sample quality and stability.
- Ligand-observed NMR: Method of choice for target engagement studies with larger targets and/or targets for which no labeling scheme is available. An additional advantage of ligand-observed NMR is that lower amounts of protein are required.
- NMR-based fragment-screening: A powerful and robust method in the field of fragment-based drug discovery, whether it is for hit identification or characterization of more advanced fragment analogs. For more details on our fragment-screening capabilities, see fragment screening.
Our NMR facility includes two 600-MHz Bruker instruments equipped with cryo-cooled probes for sensitivity and automatic sample changers for high-throughput measurements. Fast automated preparation of low-volume samples in combination with the cooling of sensitive samples makes the setup ideal for protein–ligand interaction studies by NMR.
The successful validation of early project compounds is crucial for the rapid initiation of focused follow-up activities. Left (protein-observed NMR): 2D spectra of a 15N-labeled protein exhibiting low druggability. Right (ligand-observed NMR): Saturation transfer difference (STD) NMR spectrum (red) confirming the binding of a novel allosteric inhibitor to a 150 kDa complex.