{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["17(1)"],"submitter":["Wang X"],"pubmed_abstract":["We report an enantioselective protein affinity selection mass spectrometry screening approach (E-ASMS) that enables the detection of weak binders, informs on selectivity, and generates orthogonal confirmation of binding. After method development with control proteins, we screen 31 human proteins against a designed library of 8,217 chiral compounds. We identify 16 binders to 12 targets, including many proteins predicted to be \"challenging to ligand\", and confirm their interactions through orthogonal biophysical assays. Seven binders to six targets display enantioselective binding, with K<sub>D</sub> values ranging from 3 to 20 µM. Binders for four targets (DDB1, WDR91, WDR55, and HAT1) are selected for in-depth characterization using X-ray crystallography. In all four cases, the mechanisms "],"journal":["Nature communications"],"pagination":["651"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12816581"],"repository":["biostudies-literature"],"pubmed_title":["Enantioselective protein affinity selection mass spectrometry (E-ASMS)."],"pmcid":["PMC12816581"],"pubmed_authors":["Knapp S","Chan UH","Owen DR","Ahmad S","Arrowsmith CH","Chuprina A","Ackloo S","Muller S","Matviyuk T","Yue WW","Joerger AC","Simoben CV","Santhakumar V","Edwards AM","Wang X","Dong A","Sun J","Harding R","Kondratov I","Schapira M","Li F","Mavridi D","Robbie LK","Green SR","Yang D","Houliston S","Beyett TS","Kutera M","Peng H","Brown BD","Gibson E","Silva M","Halabelian L","Bolotokova A","Brown PJ","Zeng H","Heath RB","Lenz C","Ghiabi P"],"additional_accession":[]},"is_claimable":false,"name":"Enantioselective protein affinity selection mass spectrometry (E-ASMS).","description":"We report an enantioselective protein affinity selection mass spectrometry screening approach (E-ASMS) that enables the detection of weak binders, informs on selectivity, and generates orthogonal confirmation of binding. After method development with control proteins, we screen 31 human proteins against a designed library of 8,217 chiral compounds. We identify 16 binders to 12 targets, including many proteins predicted to be \"challenging to ligand\", and confirm their interactions through orthogonal biophysical assays. Seven binders to six targets display enantioselective binding, with K<sub>D</sub> values ranging from 3 to 20 µM. Binders for four targets (DDB1, WDR91, WDR55, and HAT1) are selected for in-depth characterization using X-ray crystallography. In all four cases, the mechanisms ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-06-12T05:11:57.614Z","creation":"2026-06-12T03:07:56.517Z"},"accession":"S-EPMC12816581","cross_references":{"pubmed":["41407727"],"doi":["10.1038/s41467-025-67403-2"]}}