期刊
CHEMISTRY & BIOLOGY
卷 16, 期 11, 页码 1169-1179出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2009.10.009
关键词
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资金
- Jane Coffin Childs Foundation
- Burroughs Wellcome Career
- University of California, San Diego
- Howard Hughes Medical Institute (HHMI)
- Canadian Institutes of Health
- National Institutes of Health (NIH) [R01 GM048958, R01 GM086197, R37 NS027177]
- U.S. Army Breast Cancer Research Program (BCRP) [W81XWH-05-01-0183]
Fluorescent proteins have become valuable tools for biomedical research as protein tags, reporters of gene expression, biosensor components, and cell lineage tracers. However, applications of fluorescent proteins for deep tissue imaging in whole mammals have been constrained by the opacity of tissues to excitation light below 600 nm, because of absorbance by hemoglobin. Fluorescent proteins that excite efficiently in the optical window above 600 nm are therefore highly desirable. We report here the evolution of far-red fluorescent proteins with peak excitation at 600 nm or above. The brightest one of these, Neptune, performs well in imaging deep tissues in living mice. The crystal structure of Neptune reveals a novel mechanism for red-shifting involving the acquisition of a new hydrogen bond with the acylimine region of the chromophore.
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