Our chemical library and chemotranscriptomic screening technology are seamlessly integrated and evolve together.
As our knowledge of druggable pockets on disease-related proteins increases, our covalent chemistry-based library of small molecules expands.
Our platform has enabled us to identify hundreds of previously unknown or cryptic functional pockets on well-validated protein targets implicated in a wide range of oncologic and immunologic diseases, while simultaneously identifying compounds from our proprietary covalent chemistry library that interact in a highly selective manner with those pockets.
Our approach allows us to diversify our drug development efforts across multiple modalities, including allosteric activators and inhibitors, protein stabilizers, protein-protein interaction, or PPI, inhibitors and protein degraders.
Removing the boundaries of druggability
Despite advances in genomics, structural biology, and high-throughput screening, about 90% of disease-causing proteins cannot be targeted by current therapies due to the lack of a known addressable binding site. We are leveraging our chemoproteomic platform technology to address the key limitations of conventional screening techniques in order to discover previously unknown, or cryptic, functional pockets on the surface of proteins and identify small molecules that selectively bind to those targets.
Through a combination of our team’s chemistry, biology and drug development expertise, we are advancing a deep and diversified pipeline of highly selective small molecule therapeutics targeting high value disease-causing proteins in oncology and immunology with our lead programs targeting NRF2, STAT3 and WRN.
Our chemoproteomics platform integrates three, highly synergistic components
01
A proprietary covalent chemistry-based library of small molecules designed to selectively bind protein pockets, including cryptic and shallow pockets;
02
A novel chemoproteomic screening technology that we designed to sensitively and precisely detect small molecule interactions with any class of protein in their native cellular context at scale;
03
An integrated data portal that combines our proprietary chemoproteomic data with public databases to generate new insights into protein structure and locations of novel pockets on previously undruggable therapeutic targets.
Through our platform, we have identified several modalities to address novel pockets once they are identified, including with direct functional modulators (DFMs) or degraders.