Explore the Potential with AI-Driven Innovation
Our detailed focused library is generated on demand with advanced virtual screening and parameter assessment technology powered by the Receptor.AI drug discovery platform. This method surpasses traditional approaches, delivering compounds of better quality with enhanced activity, selectivity, and safety.
From a virtual chemical space containing more than 60 billion molecules, we precisely choose certain compounds. Our collaborator, Reaxense, aids in their synthesis and provision.
The library includes a list of the most effective modulators, each annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Furthermore, each compound is shown with its optimal docking poses, affinity scores, and activity scores, offering a detailed summary.
Our top-notch dedicated system is used to design specialised libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our methodology employs molecular simulations to explore a wide array of proteins, capturing their dynamic states both individually and within complexes. Through ensemble virtual screening, we address conformational mobility, uncovering binding sites within functional regions and remote allosteric locations. This thorough exploration ensures no potential mechanism of action is overlooked, aiming to discover novel therapeutic targets and lead compounds across an extensive spectrum of biological functions.
Our library is unique due to several crucial aspects:
partner
Reaxense
upacc
O00468
UPID:
AGRIN_HUMAN
Alternative names:
-
Alternative UPACC:
O00468; Q5SVA1; Q5SVA2; Q60FE1; Q7KYS8; Q8N4J5; Q96IC1; Q9BTD4
Background:
Agrin, a heparan sulfate basal lamina glycoprotein, is pivotal in neuromuscular junction (NMJ) formation and maintenance. It activates MUSK via the AGRN-LRP4 receptor complex, facilitating postsynaptic differentiation and AChR clustering. Agrin's role extends to modulating calcium ion homeostasis and influencing neurite outgrowth through its glycosaminoglycan chains.
Therapeutic significance:
Agrin's mutation leads to congenital myasthenic syndrome 8, characterized by neuromuscular transmission failure. Understanding Agrin's role could unveil new therapeutic strategies for treating neuromuscular disorders.