The Binding of fluorophores to proteins depends on the cellular environment

Title
The Binding of fluorophores to proteins depends on the cellular environment
Authors
김윤경이준석Xuezhi Bi하형호Shin Hui Ng안영훈이재정Bridget K. WagnerPaul A. Clemons장영태
Keywords
fluorophore; target; environment; mitochondria; CDy2; myotube; live-cell imaging; myoblast; fluorescent probes; imaging agents
Issue Date
2011-03
Publisher
Angewandte Chemie international edition
Citation
VOL 50, NO 12, 2761-2763
Abstract
Fluorescent small molecules are extensively used for live-cell imaging, but mainly in the context of labeling conjugates for other protein-binding motifs, such as antibodies.[1] As most fluorescent molecules are flat and hydrophobic, it has generally been believed that these fluorophores may bind to many hydrophobic proteins in cells without any specificity.[2] This conventional wisdom, however, has not been tested systematically because of the lack of sufficiently diverse dye sources. Recently, we developed a diversity-oriented fluorescence library approach (DOFLA) to use fluorescent dyes to distinguish directly cellular components such as GTP,[3] DNA,[4] RNA,[5] heparin,[6] and organelles.[7] In this system, the diverse structural motifs of each dye molecule in the library endowed target selectivity. From these results, we envisioned that sufficient structural modifications of fluorophore scaffold could lead us to develop probes that label specific proteins from whole proteomes.[8] As an extension of our recent finding of a fluorescein derivative labeling glutathione s-transferase,[9] here we report a rosamine derivative that labels tubulin in vitro and a mitochondrial protein in live cells.
URI
http://pubs.kist.re.kr/handle/201004/39514
ISSN
1433-7851
Appears in Collections:
KIST Publication > Article
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