期刊
BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY
卷 8, 期 -, 页码 448-455出版社
BEILSTEIN-INSTITUT
DOI: 10.3762/bjoc.8.51
关键词
fluorination; F-19 NMR; maltose-binding protein (MBP); maltose derivatives; protein interaction
资金
- Wiener Wissenschafts-, Forschungs- und Technologiefond (WWTF) [LS162]
- Grants-in-Aid for Scientific Research [23580233] Funding Source: KAKEN
A novel reporter system, which is applicable to the F-19 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 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (alpha-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (beta-gluco- and/or alpha/beta-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-ligand interaction interfaces.
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