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.
We pick out particular compounds from an extensive virtual database of more than 60 billion molecules. The preparation and shipment of these compounds are facilitated by our associate Reaxense.
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.
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.
Several key aspects differentiate our library:
partner
Reaxense
upacc
Q16635
UPID:
TAZ_HUMAN
Alternative names:
Protein G4.5
Alternative UPACC:
Q16635; A3KQT2; D3DWX2; Q5HY43; Q5HY44; Q5HY45; Q5HY48; Q86XQ6; Q86XQ7; Q86XQ8; Q86XQ9; Q86XR0
Background:
Tafazzin, also known as Protein G4.5, plays a pivotal role in the remodeling of cardiolipin, a crucial component of the mitochondrial inner membrane. This acyltransferase is essential for mitochondrial function, affecting the assembly and stability of respiratory chain complexes. Its activity includes the transacylation between various phospholipids, crucial for maintaining mitochondrial membrane dynamics and integrity.
Therapeutic significance:
Given its critical role in mitochondrial function, Tafazzin's dysfunction is directly linked to Barth syndrome, a complex X-linked disorder. Understanding Tafazzin's mechanisms offers a promising avenue for therapeutic interventions aimed at correcting mitochondrial abnormalities in Barth syndrome and potentially other mitochondrial-related diseases.