At Cedilla, we are charting new paths to target proteins that have long been outside the reach of drug discovery and development.
Approximately 50 percent of the proteome is thought to play a role in human disease and yet is not accessible by any existing or experimental drugs1
Just 10 percent of the human proteome is considered druggable by conventional therapeutic modalities1
Most new target opportunities identified in functional genomic screens cannot be inhibited by conventional pharmacological means2
Therapeutic resistance in cancer can be addressed by developing molecules with alternative modes of inhibition against known oncogenes3
The human proteome is a highly interactive and dynamic system involving thousands of proteins in constant turnover. From the moment of protein translation and folding, multiple factors contribute to a protein’s stability, including conformational states, post-translational modifications and protein-protein interactions. We are exploiting these mechanisms governing protein stability to redirect the course of disesase.
Following translation, proteins fold and go on to perform myriad functions in the cell. In response to different stimuli, protein stability is regulated by several native degradation pathways. Cedilla is embarking on a concentrated effort to understand the principles that govern protein stability with the goal of applying those principles to target proteins that drive cancer and other diseases.