Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR

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)...

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Veröffentlicht in:Beilstein journal of organic chemistry 2012-03, Vol.8 (1), p.448-455
Hauptverfasser: Braitsch, Michaela, Kählig, Hanspeter, Kontaxis, Georg, Fischer, Michael, Kawada, Toshinari, Konrat, Robert, Schmid, Walther
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Sprache:eng
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Zusammenfassung: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.
ISSN:1860-5397
1860-5397
DOI:10.3762/bjoc.8.51