Explore the Potential with AI-Driven Innovation
The specialised, focused library is developed on demand with the most recent virtual screening and parameter assessment technology, guided by the Receptor.AI drug discovery platform. This approach exceeds the capabilities of traditional methods and offers compounds with higher activity, selectivity, and safety.
The compounds are cherry-picked from the vast virtual chemical space of over 60B molecules. The synthesis and delivery of compounds is facilitated by our partner Reaxense.
Contained in the library are leading modulators, each labelled with 38 ADME-Tox and 32 physicochemical and drug-likeness qualities. In addition, each compound is illustrated with its optimal docking poses, affinity scores, and activity scores, giving a complete picture.
We employ our advanced, specialised process to create targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
It includes in-depth molecular simulations of both the catalytic and allosteric binding pockets, with ensemble virtual screening focusing on their conformational flexibility. For modulators, the process includes considering the structural shifts due to reaction intermediates to boost activity and selectivity.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
P05981
UPID:
HEPS_HUMAN
Alternative names:
Transmembrane protease serine 1
Alternative UPACC:
P05981; B2RDS4
Background:
Serine protease hepsin, also known as Transmembrane protease serine 1, is a critical enzyme that cleaves extracellular substrates, aiding in the proteolytic processing of growth factors like HGF and MST1/HGFL. It plays a pivotal role in cell growth and maintaining cell morphology, as well as in the proteolytic processing of ACE2 and urinary UMOD, essential for UMOD polymerization.
Therapeutic significance:
Understanding the role of Serine protease hepsin could open doors to potential therapeutic strategies, especially considering its involvement in crucial biological processes such as growth factor processing and cell morphology maintenance.