Nuclear Magnetic Resonance (NMR)

Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful solution-based platform for the resolution of chemical structure and target-ligand interactions.

As well as using NMR to support the synthesis activities of our Medicinal Chemistry team, Sygnature Discovery utilises this high sensitivity platform to identify weak affinity ligand-target interactions which enables site-specific compound design and optimisation of your screening strategy to accelerate your discovery program.

We have access to several cryoprobe enabled 500 – 800 MHz Bruker spectrometers facilitating enhanced sensitivity. In addition, these spectrometers are fitted with auto-samplers to enhance sample throughput for library screening.

Ligand-observed 1H Nuclear Magnetic Resonance

1H NMR is a powerful Biophysical Technique allowing tag-free identification of weak affinity interactions (low μM – mM) between a target and ligand, thus serving as an excellent platform for Fragment Screening.  By careful selection, multiple fragments can be included in a single sample, increasing throughput and reducing target material consumption. 1H NMR has the added advantage of placing no upper limit on the target protein molecular weight, meaning it can be used to study of a variety of protein target classes.

Protein-observed NMR

Protein-observed nuclear magnetic resources can be used to identify small molecule binding to a target surface and can also be used to derive binding affinities for the target-ligand interactions. Sygnature utilises this technique to generate key information to advance SAR understanding during the Hit-to-Lead and Lead Optimisation stages.

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