We are changing the status quo to make the impossible possible, by expanding the scope of new targets for drug development through targeted protein manipulation.
A second feature of our protein manipulation platform is our ability to rationally design molecular glues to hit novel disease targets. Leveraging our expertise in being able to precisely design a peptide that fits into the exact contact points of a pathological protein, we have the major advantage of exploiting the collective binding pocket that is formed by bringing two protein interfaces together. By catenating two protein-binding peptides into a single peptide molecular glue, that induce proximity between a pair of proteins, we can strengthen and stabilize pre-existing protein-protein interactions, or create de novo interactions, encouraging the binding between two proteins that would not normally interact.
Many companies use small molecules as molecular glues. In spite of many advantages of small molecules, it is still technically challenging to find a selective protein-binding small molecule. Furthermore, finding a small molecule as a molecular glue that selectively binds to two target proteins simultaneously is even more technically challenging. In contrast, it is relatively easier and faster to find peptides that selectively bind to target proteins.
Most molecular glues are designed to stick a target protein to a ligase that triggers degradation. In our case, we design our molecular glues to stick any two proteins together. Therefore, our peptide molecular glues not only can trigger protein degradation, but also have many other applications, including, but not limited to, protein stabilization and phosphorylation.
We are still in the early stages of this technology, as are many companies. However, by gluing any two proteins together, we are forging a new path for unlocking more undruggable proteins to be targeted.
Two protein-binding peptides catenated into a single peptide, inducing proximity between a pair of proteins. This strengthens and stabilizes pre-existing protein-protein interactions, or creates de novo interactions, encouraging the binding between two proteins that would not normally interact.