A Europium Complex That Selectively Stains Nucleoli of Cells

A europium complex selectively staining the nucleolus of NIH 3T3, HeLa, and HDF cells is reported. This complex possesses not only the advantage of the long lifetime of europium emission (0.3 ms), but also a chromophore that allows excitation at a relatively long wavelength (λmax = 384 nm) and gives...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2006-02, Vol.128 (7), p.2294-2299
Main Authors: Yu, Junhua, Parker, David, Pal, Robert, Poole, Robert A, Cann, Martin J
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Cell Nucleolus - chemistry
Cell Nucleolus - metabolism
Cell structures and functions
Europium - chemistry
Europium - metabolism
Europium - pharmacokinetics
Fundamental and applied biological sciences. Psychology
Heterocyclic Compounds - chemistry
Humans
Luminescent Measurements - methods
Mice
Molecular and cellular biology
NIH 3T3 Cells
Organometallic Compounds - chemistry
Organometallic Compounds - metabolism
Organometallic Compounds - pharmacokinetics
Ribosome
Staining and Labeling - methods
Thioxanthenes - chemistry
Xanthones - chemistry
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Summary:A europium complex selectively staining the nucleolus of NIH 3T3, HeLa, and HDF cells is reported. This complex possesses not only the advantage of the long lifetime of europium emission (0.3 ms), but also a chromophore that allows excitation at a relatively long wavelength (λmax = 384 nm) and gives rise to an acceptable quantum yield (9%). The complex can be used both in live cell and fixed cell imaging, giving an average intracellular concentration on the order of 0.5 μM. Strong binding to serum albumin has been demonstrated by examination of the analogous gadolinium complex, studying relaxivity changes with increasing protein concentration. The intracellular speciation of the complex has been examined by circularly polarized emission spectroscopy and is consistent with the presence of more than one europium species, possibly protein bound.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja056303g