Small Molecule Drug Discovery

Allosteric & Orthosteric Therapeutics

Only Fox® Radical Protein Footprinting (FRPF) rapidly enables the identification of the therapeutic binding site as well as target response at the amino acid level, enabling researchers to promote promising leads while killing those that inappropriately bind or elicit no or an undesired target response.

In the pursuit of allosteric and orthosteric small-molecule therapeutics, high-throughput (HT) primary screening rapidly identifies initial hits from chemical libraries, often through fragment-based drug discovery. However, distinguishing specific, high-affinity binders from non-productive interactions remains a major challenge.

The Fox Radical Protein Footprinting platform transforms secondary screening by unambiguously identifying therapeutic binding sites and characterizing target response upon drug engagement. This capability ensures that only promising leads advance while eliminating compounds that fail to bind appropriately or induce the desired allosteric effect.

During lead optimization, chemical modifications are introduced to enhance specificity and binding affinity. Fox Radical Protein Footprinting provides residue-level precision, confirming whether optimized leads retain productive target engagement and response.

Compared to ultra high-resolution techniques like cryo-EM, NMR and crystallography—all of which are time- and resource-intensive — Fox Footprinting delivers actionable structural insights within days, empowering medicinal chemistry, SAR studies, and rational drug design with unprecedented efficiency.

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