title: Synthesis of fluorinated maltose derivatives for monitoring protein interaction by (19)F NMR.
abstract: A novel reporter system, which is applicable to the (19)F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein-ligand or protein-protein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both (19)F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (α-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (β-gluco- and/or α/β-manno-type) are utilized as internal references. Moreover, this reporter system was used for relative affinity studies of fluorinated and nonfluorinated carbohydrates to the maltose-binding protein, which were found to be in perfect agreement with published X-ray data. The results of the NMR competition experiments together with the established correlation between (19)F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein-ligand interaction interfaces.
authors.affiliation: Department of Organic Chemistry, University of Vienna, Währinger Strasse 38, A-1090 Vienna, Austria.
authors.forename: Michaela
authors.initials: M
authors.lastname: Braitsch
authors.forename: Hanspeter
authors.initials: H
authors.lastname: Kählig
authors.forename: Georg
authors.initials: G
authors.lastname: Kontaxis
authors.forename: Michael
authors.initials: M
authors.lastname: Fischer
authors.forename: Toshinari
authors.initials: T
authors.lastname: Kawada
authors.forename: Robert
authors.initials: R
authors.lastname: Konrat
authors.forename: Walther
authors.initials: W
authors.lastname: Schmid