More than 10% of the human proteome contains PRM-binding domains – a class of protein-domains specialized in the recognition of proline-rich motifs.
These domains are involved in a multitude of pathologies, such as cancer, Alzheimer’s and other neurodegenerative diseases, cardiovascular diseases, immune-meditated disorders, etc.
However, they are so far considered as “undruggable”, making peptidomimetic and small molecule competitors of PRM urgently needed.
Through a unique design concept, PROSION established a platform of synthetic Proline-derived modules (ProMs) as the world’s first validated and patented PRM-structure mimicking scaffolds. As stereo-defined building blocks, these can be assembled into urgently needed competitors of PRM.
Based on this disruptive technology, PROSION is able to develop first-in-class small molecule drugs, for a particularly abundant class of undruggables – finally making PRM binding domains druggable.
We are striving to push our own drug compounds through pre-clinical and clinical development. The first candidate that we are developing is a highly selective ProM-based inhibitor for addressing solid tumor cancer metastasis.
While this is the first POC, the platform has the potential to address various targets and indications.
If you are interested in becoming part of this exciting journey, please head to our contact page.
ProMs are the first reported and patented mimetics of a very abundant secondary structure of our organism and have thus a vast use-potential in a multitude of areas next to drug discovery (e.g. PROTACs, Biotools, etc.).
We therefore offer a broad range of ProMs, enabling our potential partners to gain an in-depth scientific understanding.
If you are interested in working with our ProMs, please head to our contact page.
Designed nanomolar small-molecule inhibitors of Ena/VASP EVH1 interaction impair invasion and extravasation of breast cancer cells
Triple‐Helix‐Stabilizing Effects in Collagen Model Peptides Containing PPII‐Helix‐Preorganized Diproline Modules
Design and Synthesis of Building Blocks for PPII‐Helix Secondary‐Structure Mimetics: A Stereoselective Entry to 4‐Substituted 5‐Vinylprolines
A modular toolkit to inhibit proline-rich motif–mediated protein–protein interactions