{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jordan C"],"funding":["Studienstiftung des Deutschen Volkes","Westf?lische Wilhelms-Universit?t M?nster","Gottfried Wilhelm Leibniz Universit?t Hannover","European Research Council","Deutsche Forschungsgemeinschaft","Fonds der Chemischen Industrie","Eidgen?ssische Technische Hochschule Z?rich"],"pagination":["1481-1489"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11363330"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(8)"],"pubmed_abstract":["Carbohydrates regulate an inimitable spectrum of biological functions, yet successfully leveraging this therapeutic avenue continues to be frustrated by low affinities with glycan-specific proteins. A conspicuous exception is the interaction of monosialotetrahexosylganglioside (GM1) with the carbohydrate-recognition domain of cholera toxin from <i>Vibrio cholerae</i>: this is one of the strongest protein-carbohydrate interactions known. To establish the importance of a long-discussed key hydrogen bond between C2 of the terminal galactose of GM1 and the B subunit pentamer of cholera toxin (CTB<sub>5</sub>), the total synthesis of a selectively fluorinated GM1 epitope was conducted in 19 steps. This process of molecular editing (O<sup>δ-</sup>H → F<sup>δ-</sup>) strategically deletes the hyd"],"journal":["ACS central science"],"pubmed_title":["Probing the Origin of Affinity in the GM1-Cholera Toxin Complex through Site-Selective Editing with Fluorine."],"pmcid":["PMC11363330"],"funding_grant_id":["101002326","818949","951459","37 19-2"],"pubmed_authors":["Teschers CS","Pape F","Jordan C","Bussmann K","Hayashi T","Kohnke J","Aufiero M","Lobbert A","Axer A","Gilmour R","Bergander K","Campbell E","Fan J","Siebold K","Gossert AD"],"additional_accession":[]},"is_claimable":false,"name":"Probing the Origin of Affinity in the GM1-Cholera Toxin Complex through Site-Selective Editing with Fluorine.","description":"Carbohydrates regulate an inimitable spectrum of biological functions, yet successfully leveraging this therapeutic avenue continues to be frustrated by low affinities with glycan-specific proteins. A conspicuous exception is the interaction of monosialotetrahexosylganglioside (GM1) with the carbohydrate-recognition domain of cholera toxin from <i>Vibrio cholerae</i>: this is one of the strongest protein-carbohydrate interactions known. To establish the importance of a long-discussed key hydrogen bond between C2 of the terminal galactose of GM1 and the B subunit pentamer of cholera toxin (CTB<sub>5</sub>), the total synthesis of a selectively fluorinated GM1 epitope was conducted in 19 steps. This process of molecular editing (O<sup>δ-</sup>H → F<sup>δ-</sup>) strategically deletes the hyd","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2026-06-01T16:15:33.884Z","creation":"2025-04-06T13:44:35.022Z"},"accession":"S-EPMC11363330","cross_references":{"pubmed":["39220706"],"doi":["10.1021/acscentsci.4c00622"]}}