%0 Journal Article
%T Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR
%A Michaela Braitsch
%A Hanspeter K£¿hlig
%A Georg Kontaxis
%A Michael Fischer
%J Beilstein Journal of Organic Chemistry
%D 2012
%I 
%R 10.3762/bjoc.8.51
%X A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein¨Cligand or protein¨Cprotein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (¦Á-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (¦Â-gluco- and/or ¦Á/¦Â-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 19F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein¨Cligand interaction interfaces.
%K fluorination
%K 19F NMR
%K maltose-binding protein (MBP)
%K maltose derivatives
%K protein interaction
%U http://dx.doi.org/10.3762/bjoc.8.51