期刊
JOURNAL OF ORGANIC CHEMISTRY
卷 74, 期 19, 页码 7309-7314出版社
AMER CHEMICAL SOC
DOI: 10.1021/jo901369k
关键词
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资金
- NIH Cell Migration Consortium [GM064346]
- A.M. Escudero Foundation postdoctoral fellowship
- Department of Chemistry Instrumentation Facility [NIH-1S10RR013886-01]
Protein phosphorylation is a ubiquitous post-translational modification, and protein kinases, the enzymes that catalyze the phosphoryl transfer, are involved in nearly every aspect of normal, as well as aberrant, cell function. Here we describe the synthesis of novel. red-shifted 8-hydroxyquinoline-based fluorophores and their incorporation into peptidyl kinase activity reporters. Replacement of the sulfonamide group of the sulfonamido-oxine (1, Sox) chromophore, which has been previously used In kinase sensing, by a 1,4-substituted triazole moiety prepared via click chemistry resulted in a significant bathochromic shift in the fluorescence excitation (15 nm) and emission (40 rim) maxima for the Mg2+ chelate. Furthermore, when a click derivative was incorporated into a chemosensor for MK2, the kinase accepted the new substrate as efficiently as the previously reported Sox-based sensor. Taken together, these results extend the utility range of kinase sensors that are based on chelation-enhanced fluorescence (CHEF).
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