Explore the Potential with AI-Driven Innovation
The focused library is created on demand with the latest virtual screening and parameter assessment technology, supported by the Receptor.AI drug discovery platform. This method is more effective than traditional methods and results in higher-quality compounds with better activity, selectivity, and safety.
Our selection of compounds is from a large virtual library of over 60 billion molecules. The production and distribution of these compounds are managed by our partner Reaxense.
In the library, a selection of top modulators is provided, each marked with 38 ADME-Tox and 32 parameters related to physicochemical properties and drug-likeness. Also, every compound comes with its best docking poses, affinity scores, and activity scores, providing a comprehensive overview.
We utilise our cutting-edge, exclusive workflow to develop focused libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our methodology leverages molecular simulations to examine a vast array of proteins, capturing their dynamics in both isolated forms and in complexes with other proteins. Through ensemble virtual screening, we thoroughly account for the protein's conformational mobility, identifying critical binding sites within functional regions and distant allosteric locations. This detailed exploration ensures that we comprehensively assess every possible mechanism of action, with the objective of identifying novel therapeutic targets and lead compounds that span a wide spectrum of biological functions.
Several key aspects differentiate our library:
partner
Reaxense
upacc
Q9UHN6
UPID:
CEIP2_HUMAN
Alternative names:
Cell migration-inducing hyaluronidase 2; Transmembrane protein 2
Alternative UPACC:
Q9UHN6; A6H8W9; B2RTQ6; Q5T838; Q5T839; Q5T840; Q5T841; Q8NBP6; Q9P2D5
Background:
Inactive cell surface hyaluronidase CEMIP2, also known as Cell migration-inducing hyaluronidase 2 and Transmembrane protein 2, plays a pivotal role in hyaluronan metabolism. It regulates the expression of CEMIP and HAS2, key enzymes in HA synthesis and depolymerization, respectively, despite lacking catalytic hyaluronic acid-degrading activity.
Therapeutic significance:
Understanding the role of Inactive cell surface hyaluronidase CEMIP2 could open doors to potential therapeutic strategies.