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.
We carefully select specific compounds from a vast collection of over 60 billion molecules in virtual chemical space. Our partner Reaxense helps in synthesizing and delivering these compounds.
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.
Our top-notch dedicated system is used to design specialised libraries.
Fig. 1. The sreening workflow of Receptor.AI
By deploying molecular simulations, our approach comprehensively covers a broad array of proteins, tracking their flexibility and dynamics individually and within complexes. Ensemble virtual screening is utilised to take into account conformational dynamics, identifying pivotal binding sites located within functional regions and at allosteric locations. This thorough exploration ensures that every conceivable mechanism of action is considered, aiming to identify new therapeutic targets and advance lead compounds throughout a vast spectrum of biological functions.
Our library is unique due to several crucial aspects:
partner
Reaxense
upacc
O43451
UPID:
MGA_HUMAN
Alternative names:
Alpha-1,4-glucosidase
Alternative UPACC:
O43451; E7ER45; Q0VAX6; Q75ME7; Q86UM5
Background:
Maltase-glucoamylase, identified by the accession number O43451, plays a pivotal role in the digestive system. This enzyme, also known as Alpha-1,4-glucosidase, is crucial for the breakdown of dietary starch oligosaccharides in the small intestine. It specifically targets the non-reducing alpha-(1,4)-linked glucose residue in linear dextrins, preserving the anomeric center stereochemistry. Its ability to hydrolyze short length oligomaltoses, ranging from two to seven glucose residues, alongside its lower efficiency in cleaving alpha-(1,2), alpha-(1,3), and alpha-(1,6) glycosidic linkages, underscores its specificity and importance in carbohydrate metabolism.
Therapeutic significance:
Understanding the role of Maltase-glucoamylase could open doors to potential therapeutic strategies.