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.
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.
Our high-tech, dedicated method is applied to construct targeted 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.
Key features that set our library apart include:
partner
Reaxense
upacc
O00214
UPID:
LEG8_HUMAN
Alternative names:
Po66 carbohydrate-binding protein; Prostate carcinoma tumor antigen 1
Alternative UPACC:
O00214; O15215; Q5T3P5; Q5T3Q4; Q8TEV1; Q96B92; Q9BXC8; Q9H584; Q9H585; Q9UEZ6; Q9UP32; Q9UP33; Q9UP34
Background:
Galectin-8, identified by its alternative names Po66 carbohydrate-binding protein and Prostate carcinoma tumor antigen 1, is a beta-galactoside-binding lectin. It plays a crucial role in sensing membrane damage caused by infection, thereby restricting the proliferation of pathogens by targeting them for autophagy. Galectin-8 detects membrane rupture by binding to beta-galactoside ligands exposed to the cytoplasm following rupture. It is pivotal in initiating autophagy via interaction with CALCOCO2/NDP52, essential for combating bacterial invasions like S.typhimurium and Picornaviridae viruses. Galectin-8 shows a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.
Therapeutic significance:
Understanding the role of Galectin-8 could open doors to potential therapeutic strategies.