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Fragment Screening 

1H and 19F screen of low molecular weight fragments by NMR. Ranking of hits is performed according to consensus binding between different NMR experiments. Use our curated libraries or bring your own.

⦾ Curated Fragment Librairies

Our 1H and 19F fragment libraries went through rigorous cheminformatics filtering and exhaustive NMR curation to retain only well-behaved and drug-like compounds.

⦾ Optimized Pooling 

Our curated fragment libraries are screened as mixtures of fragments in order to increase throughput, allowing for a streamlined evaluation of the binding of thousands of drug-like fragments to your target.

Ligand Binding Studies

NMR binding studies ranging from a single experiment to a consensus-based approach combining various experiments. Compounds are ranked by scores to guide medicinal chemistry efforts.

⦾ 1H Ligand-Detection
⦾ 19F Ligand-Detection
⦾ Protein-Detected NMR

Allows for a more exhaustive evaluation of binding, sample integrity, compound concentration and binding epitope.

The highly sensitive fluorine atom allows for fast, background-free detection of a wide range of binding events.

Higher affinity compounds can sometimes be missed by ligand-observed techniques. Monitoring protein fingerprints helps bridge the gap between ligand-detected NMR and other biophysical techniques, while keeping track of protein integrity.

Compound Solution Behavior Characterization

Solubility and aggregation assessment of compounds to guide experimental testing and control for a major source of artifacts.

⦾ Aggregation

Relaxation, dilution and detergent effect assays are performed to get the most accurate picture of the behavior of compounds of interest in solution.

⦾Accurate Concentration Determination

The actual compound concentration of each sample is systematically determined using the data gathered during any kind of NMR experiment. It can also be independently measured as part of a solution behavior routine. 

Kd by NMR

Detection of a binding event by the perturbation of the target protein residues. By following these residues in NMR during a titration experiment with the ligand of interest,  Kd in the  mM to low μM range can be determined with or without knowing the identity of the perturbed residues.

Kd and Stoichiometry

Extraction of binding affinity constants from protein-detected or ligand-detected NMR experiments.

Target Binding Site Identification

Mapping the binding site(s) of compounds of interests on a target using direct or indirect NMR experiments.

Chemical Shift Mapping

Competition Assays with Tool Compound

Direct identification by NMR of perturbed target residues upon addition of a compound of interest.

Inference of the binding site of a molecule using competition assays with tool compounds with known binding modes.

Get to Know Your Target

Characterization of the target protein folding, stability, promiscuity and optimal concentration for the screening process by 1D NMR assays. Make sure the target is well-behaved and warrants further examination.

NMR Based Target Enablement

Assessment of several intrinsic parameters of the target protein using NMR experiments.


Accelerate Your Path to Discovery

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