{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liang S"],"funding":["Funding of Taizhou People’s Hospital (Taizhou, Jiangsu, China"],"pagination":["2241118"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10399481"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["38(1)"],"pubmed_abstract":["Prostate cancer (PCa) is a clinically heterogeneous disease with a progressively increasing incidence. Concurrent inhibition of coactivator-associated arginine methyltransferase 1 (CARM1) and histone deacetylase 2 (HDAC2) could potentially be a novel strategy against PCa. Herein, we identified seven compounds simultaneously targeting CARM1 and HDAC2 through structure-based virtual screening. These compounds possessed potent inhibitory activities at the nanomolar level <i>in vitro</i>. Among them, CH-1 was the most active inhibitor which exhibited excellent and balanced inhibitory effects against both CARM1 (IC<sub>50</sub> = 3.71 ± 0.11 nM) and HDAC2 (IC<sub>50</sub> = 4.07 ± 0.25 nM). MD simulations presented that CH-1 could stably bind the active pockets of CARM1 and HDAC2. Notably, CH-1"],"journal":["Journal of enzyme inhibition and medicinal chemistry"],"pubmed_title":["Discovery and biological evaluation of novel CARM1/HDAC2 dual-targeting inhibitors with anti-prostate cancer agents."],"pmcid":["PMC10399481"],"funding_grant_id":["ZL202005","QDJJ202101"],"pubmed_authors":["Liang S","Niu MM","Li J","Yang L","Zhang Y","He W","Geng Y","Xu Z"],"additional_accession":[]},"is_claimable":false,"name":"Discovery and biological evaluation of novel CARM1/HDAC2 dual-targeting inhibitors with anti-prostate cancer agents.","description":"Prostate cancer (PCa) is a clinically heterogeneous disease with a progressively increasing incidence. Concurrent inhibition of coactivator-associated arginine methyltransferase 1 (CARM1) and histone deacetylase 2 (HDAC2) could potentially be a novel strategy against PCa. Herein, we identified seven compounds simultaneously targeting CARM1 and HDAC2 through structure-based virtual screening. These compounds possessed potent inhibitory activities at the nanomolar level <i>in vitro</i>. Among them, CH-1 was the most active inhibitor which exhibited excellent and balanced inhibitory effects against both CARM1 (IC<sub>50</sub> = 3.71 ± 0.11 nM) and HDAC2 (IC<sub>50</sub> = 4.07 ± 0.25 nM). MD simulations presented that CH-1 could stably bind the active pockets of CARM1 and HDAC2. Notably, CH-1","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Dec","modification":"2025-04-27T00:20:29.609Z","creation":"2025-04-06T17:49:28.821Z"},"accession":"S-EPMC10399481","cross_references":{"pubmed":["37528657"],"doi":["10.1080/14756366.2023.2241118"]}}