Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.07.29.226308v1?rss=1 Authors: Joel, I. y., Adigun, T. O., AJIBOLA, A. O., BANKOLE, O. O., OZOJIOFOR, U. O., REMI-ESAN, I. A., SULAIMON, L. A. Abstract: Evading apoptosis is one of the hallmarks of cancer cells, therefore a lot of therapeutic strategies have been developed to induce cell death in these cells. BCL2 family protein governs the intrinsic pathway of cell death. The BCL2 family protein possess both pro and anti-apoptosis members. BCL2 protein, a pioneering member of the anti-apoptosis protein has been implicated in several cancerous cells; with dozens of small-molecule inhibitors developed to inhibit its activity. BCL2 family protein processes BH domains (1-4) for heterodimerization and homodimerization amidst it family members and targeting the BH4 domain is an established new strategy for cancer therapy; however, only BDA366 has been reported so far as a BH4 binding molecule. Using Computer-aided drug discovery techniques (Molecular docking, QM-polarized docking, Induced-fit docking, QM-MM optimization, and QM electronic descriptors) we screened M sample (~ 99,000 compounds) of the SCUBIDOO database to find ligands that interact with the BH4 domain of BCL2 protein with high affinity, we identified 11 putative BH4 specific small molecules with binding affinity ranging from ~ -84kcal/mol to -64kcal/mol with a putative binding hypothesis with BH4 amino acid residues: ASP10, ARG12, GLU13, MET16, LYS17, and HIS20 Copy rights belong to original authors. Visit the link for more info