期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 130, 期 41, 页码 13630-13638出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja804754y
关键词
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资金
- NSF [CHE-0414243]
- NIH Cell Migration Consortium [GM064346]
- Biotechnology Training Program [T32-GM08334]
- Department of Chemistry Instrumentation Facility [NSF CHE-9808061, DBI-9729592, CHE-0234877]
- Biophysical Instrumentation Facility for the Study of Complex Macromolecular Systems [NSF-0070319]
We have developed a new unnatural amino acid based on the solvatochromic fluorophore 4-N,N-dimethylamino-1,8-naphthalimide (4-DMN) for application in the study of protein-protein interactions. The fluorescence quantum yield of this chromophore is highly sensitive to changes in the local solvent environment, demonstrating switch-like emission properties characteristic of the dimethylaminophthalimide family of fluorophores. In particular, this new species possesses a number of significant advantages over related fluorophores, including greater chemical stability under a wide range of conditions, a longer wavelength of excitation (408 nm), and improved synthetic accessibility. This amino acid has been prepared as an Fmoc-protected building block and may readily be incorporated into peptides via standard solid-phase peptide synthesis. A series of comparative studies are presented to demonstrate the advantageous properties of the 4-DMN amino acid relative to those of the previously reported 4-N,N-dimethylaminoph-thalimidoalanine and 6-N,N-dimethylamino-2,3-naphthalimidoalanine amino acids. Other commercially available solvatochromic fluorophores are also include in these studies. The potential of this new probe as a tool for the study of protein-protein interactions is demonstrated by introducing it into a peptide that is recognized by calcium-activated calmodulin. The binding interaction between these two components yields an increase in fluorescence emission greater than 900-fold.
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