What NMR settles
NMR changes what a decision rests on. It confirms, on the molecules themselves, that a hit engages its target, so a series is built on a validated interaction rather than only on an assay signal. It locates the binding site and the binding mode, which gives medicinal chemistry a clear direction rather than a hypothesis. And it reads how a candidate behaves in solution at the concentration it will be dosed at, so solubility and aggregation surface early enough to act on.
That range comes from one technique on one sample. Structure, dynamics, kinetics and affinity are measured together, in solution, which is why NMR equally contributes to hit finding as well has hit to lead and lead optimization pre-clinical stages.
A fragment library built for NMR
Around 2,500 highly soluble fragments, designed on the rule of three and then pushed deliberately toward three-dimensional character and shape diversity rather than flat, easy chemistry.
Every fragment is qualified individually for integrity, solubility, reference chemical shifts and reference spectra. Suitable for both 1H and 19F screening, the library is ready to be deployed against protein or nucleic acid targets to identify high-quality starting ligands that can be readily expanded, optimized, or merged into more potent binders.
Labeled protein, produced and characterized at the same site
Protein-observed NMR starts with the protein.
Construct design, bacterial expression, purification, and quality control are performed by the same team that conducts NMR studies, enabling rapid, efficient, and highly coordinated project execution. Because the scientists who design and produce the protein are also responsible for the downstream NMR experiments, allowing labeling strategies, buffer systems and experimental conditions to be optimized early for the highest-quality spectra for project success.
Four high-field Bruker instruments serve the work, two of them cryo-probe equipped, with automated sample changers for screening campaigns.
Whether embedded within a fully integrated drug discovery program or delivered as a stand-alone service, our scientists work in close partnership with chemistry, biology, and DMPK teams to accelerate decision-making and project progression. Flexible in scope, never fragmented in team.
Move faster from target to preclinical candidate
IRBM’s Integrated Drug Discovery platform unites chemistry, biology, DMPK, and in vivo pharmacology under one scientific framework so candidates advance through fewer handoffs, stronger data continuity, and better-informed decisions.
Frequently asked questions
What does NMR settle that other biophysical methods do not?
Biophysical methods such as SPR and BLI measure binding affinities and kinetics, but do not provide atomic resolution information. Crystallography shows one static conformation, in the crystal state. NMR reports binding, location, affinity, conformation and motion on the same sample in solution, and it is often the only option for intrinsically disordered proteins, flexible regions, small transmembrane proteins and nucleic acids, where a crystal is not available and the target is too small for single-particle cryo-EM.
Do you need isotopically labeled protein, and can you produce it?
Ligand-observed NMR experiments, including fragment screening, need no labeled protein and no target structure. Protein-observed NMR experiments does, and isotopically labeled protein is produced by the same team who runs the NMR spectrometers, from construct design through purification and quality control.
Can you screen fragments without a structure of the target?
Yes. Ligand-observed NMR screening detects binding without assigned spectra or a solved structure. Structural information can follow once hits are confirmed, if the target supports it.
How does NMR fit alongside a screening cascade already running elsewhere?
NMR is routinely used as the orthogonal check on hits from high-throughput and virtual screens, and as the method that explains why a compound in an existing series behaves the way it does. It works as a standalone service or inside an integrated drug discovery program.
What instruments are installed, and how is project data handled?
Four high-field Bruker spectrometers: two 600 MHz, both equipped with cryo-probes, one 500 MHz and one 400 MHz, all with automated sample changers for screening campaigns. Configurations cover bio-NMR observation of 1H, 13C, 15N, and other multinuclear observation including 19F, with full variable temperature control. All project data, materials and results remain the property of the client under confidentiality agreement, and the work is carried out at a single research site in Rome, Italy.
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