Our Powerful Engine to Naturally Destroy Disease-Causing Proteins
Our bodies have a natural mechanism — proteasomal degradation — for disposing of unwanted proteins. During this process, ubiquitin, a small, regulatory molecule found in almost all human cells, attaches to a protein and signals the protein transport machinery to ferry it to the proteasome for degradation and disposal.
Targeted protein degradation, which harnesses this ubiquitin-proteasome machinery to completely remove disease-causing proteins, is viewed by many as the most promising new therapeutic modality since CRISPR gene editing and RNAi therapeutics. It involves designing small molecules with two active ends: one that binds to the target protein of interest and the other to the right E3 ubiquitin ligase.
Kymera takes a systematic and rational approach to designing these molecules using our Pegasus™ platform. By continually increasing our understanding of how protein degradation works, we accelerate access to novel E3 ligase biology and binders, become more effective in identifying druggable targets likely to benefit from therapeutic intervention and discover and develop potent and specific drugs in a disease agnostic manner.
Algorithm-based prediction model
Proprietary E3 Ligase toolbox
State-of-the-art degradation assays
Premier in silico & structural biology
Comprehensive ligandability assessment
Expanding the Druggable Universe
Conventional small-molecule and antibody drugs can access only about 10-20% of the proteins in the human body. In addition, though the ubiquitin-proteasome process has more than 600 E3 ligases, only a handful of them have been liganded. Our novel E3 ligase/binder identification capabilities open a vast and fertile territory to discover drug candidates for many intractable diseases that other therapeutic modalities cannot address.