{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sharifzadeh S"],"funding":["Department of Chemistry, University of Minnesota","University of Minnesota","NCI NIH HHS","Alfred P. Sloan Foundation","National Institute of General Medical Sciences","NIH HHS","NIGMS NIH HHS"],"pagination":["1242-1251"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7784776"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(5)"],"pubmed_abstract":["Selective chemical probes enable individual investigation of penicillin-binding proteins (PBPs) and provide critical information about their enzymatic activity with spatial and temporal resolution. To identify scaffolds for novel probes to study peptidoglycan biosynthesis in <i>Bacillus subtilis</i>, we evaluated the PBP inhibition profiles of 21 β-lactam antibiotics from different structural subclasses using a fluorescence-based assay. Most compounds readily labeled PBP1, PBP2a, PBP2b, or PBP4. Almost all penicillin scaffolds were coselective for all or combinations of PBP2a, 2b, and 4. Cephalosporins, on the other hand, possessed the lowest IC<sub>50</sub> values for PBP1 alone or along with PBP4 (ceftriaxone, cefoxitin) and 2b (cefotaxime) or 2a, 2b, and 4 (cephalothin). Overall, five s"],"journal":["ACS chemical biology"],"pubmed_title":["Harnessing β-Lactam Antibiotics for Illumination of the Activity of Penicillin-Binding Proteins in <i>Bacillus subtilis</i>."],"pmcid":["PMC7784776"],"funding_grant_id":["P30 CA077598","R01 GM128439","R35 GM131783","DP2 OD008592","R01 GM128439-01A1"],"pubmed_authors":["Kearns DB","Dempwolff F","Sharifzadeh S","Carlson EE"],"additional_accession":[]},"is_claimable":false,"name":"Harnessing β-Lactam Antibiotics for Illumination of the Activity of Penicillin-Binding Proteins in <i>Bacillus subtilis</i>.","description":"Selective chemical probes enable individual investigation of penicillin-binding proteins (PBPs) and provide critical information about their enzymatic activity with spatial and temporal resolution. To identify scaffolds for novel probes to study peptidoglycan biosynthesis in <i>Bacillus subtilis</i>, we evaluated the PBP inhibition profiles of 21 β-lactam antibiotics from different structural subclasses using a fluorescence-based assay. Most compounds readily labeled PBP1, PBP2a, PBP2b, or PBP4. Almost all penicillin scaffolds were coselective for all or combinations of PBP2a, 2b, and 4. Cephalosporins, on the other hand, possessed the lowest IC<sub>50</sub> values for PBP1 alone or along with PBP4 (ceftriaxone, cefoxitin) and 2b (cefotaxime) or 2a, 2b, and 4 (cephalothin). Overall, five s","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 May","modification":"2025-04-22T03:02:20.293Z","creation":"2025-04-05T20:34:13.197Z"},"accession":"S-EPMC7784776","cross_references":{"pubmed":["32155044"],"doi":["10.1021/acschembio.9b00977"]}}