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.
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.
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 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
Q12934
UPID:
BFSP1_HUMAN
Alternative names:
Beaded filament structural protein 1; Lens fiber cell beaded-filament structural protein CP 115; Lens intermediate filament-like heavy
Alternative UPACC:
Q12934; F5H0G1; O43595; O76034; O95676; Q8IVZ6; Q9HBX4
Background:
Filensin, also known as Beaded filament structural protein 1, plays a crucial role in the formation of lens intermediate filaments, essential for eye lens transparency. It forms a complex with BFSP1, BFSP2, and CRYAA, vital for lens structure integrity (PubMed:28935373). Additionally, Filensin is involved in modulating the calcium regulation of MIP water permeability, highlighting its significance in lens physiology (PubMed:30790544).
Therapeutic significance:
Filensin's mutation is directly linked to Cataract 33, multiple types, characterized by juvenile-onset opacities in the lens cortex. Understanding the role of Filensin could open doors to potential therapeutic strategies for cataract treatment, emphasizing the importance of targeted genetic research in ophthalmology.