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Development of Functional Fluorescent Molecular Probes for the Detection of Biological Substances.

Suzuki Y, Yokoyama K - Biosensors (Basel) (2015)

Bottom Line: This review is confined to sensors that use fluorescence to transmit biochemical information.Fluorescence is, by far, the most frequently exploited phenomenon for chemical sensors and biosensors.To achieve selective (bio)molecular recognition based on these fluorescence phenomena, various fluorescent elements such as small organic molecules, enzymes, antibodies, and oligonucleotides have been designed and synthesized over the past decades.

View Article: PubMed Central - PubMed

Affiliation: Health Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Central 6, 1-1-1 Higashi, Tsukuba 305-8566, Japan. suzuki-yoshio@aist.go.jp.

ABSTRACT
This review is confined to sensors that use fluorescence to transmit biochemical information. Fluorescence is, by far, the most frequently exploited phenomenon for chemical sensors and biosensors. Parameters that define the application of such sensors include intensity, decay time, anisotropy, quenching efficiency, and luminescence energy transfer. To achieve selective (bio)molecular recognition based on these fluorescence phenomena, various fluorescent elements such as small organic molecules, enzymes, antibodies, and oligonucleotides have been designed and synthesized over the past decades. This review describes the immense variety of fluorescent probes that have been designed for the recognitions of ions, small and large molecules, and their biological applications in terms of intracellular fluorescent imaging techniques.

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Chemical structure of a fluorescent molecular probe for the labeling of cysteine in proteins.
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biosensors-05-00337-f012: Chemical structure of a fluorescent molecular probe for the labeling of cysteine in proteins.

Mentions: Tsien et al. reported a site-specific fluorescent labeling reagent for recombinant proteins in living cells (Figure 12) [77]. The sequence Cys-Cys-Xaa-Xaa-Cys-Cys, where Xaa is a noncysteine amino acid, is genetically fused to or inserted within the protein, where it can be specifically recognized by FlAsH. FlAsH is a membrane-permeant fluorescein derivative with two As(III) substituents, which fluoresces only after the arsenics bind to the cysteine thiols in the target sequence. The in vitro affinities and detection limits in living cells are optimized with Xaa-Xaa = Pro-Gly, suggesting that the preferred peptide conformation is a hairpin rather than the previously proposed R-helix. Many analogues of FlAsH have now been synthesized, including ReAsH, a resorufin derivative which is excitable at 590 nm and red fluorescent. These analogous biarsenicals enable affinity chromatography, fluorescence anisotropy measurements, and electron-microscopic localization of tetracysteine-tagged proteins.


Development of Functional Fluorescent Molecular Probes for the Detection of Biological Substances.

Suzuki Y, Yokoyama K - Biosensors (Basel) (2015)

Chemical structure of a fluorescent molecular probe for the labeling of cysteine in proteins.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4493553&req=5

biosensors-05-00337-f012: Chemical structure of a fluorescent molecular probe for the labeling of cysteine in proteins.
Mentions: Tsien et al. reported a site-specific fluorescent labeling reagent for recombinant proteins in living cells (Figure 12) [77]. The sequence Cys-Cys-Xaa-Xaa-Cys-Cys, where Xaa is a noncysteine amino acid, is genetically fused to or inserted within the protein, where it can be specifically recognized by FlAsH. FlAsH is a membrane-permeant fluorescein derivative with two As(III) substituents, which fluoresces only after the arsenics bind to the cysteine thiols in the target sequence. The in vitro affinities and detection limits in living cells are optimized with Xaa-Xaa = Pro-Gly, suggesting that the preferred peptide conformation is a hairpin rather than the previously proposed R-helix. Many analogues of FlAsH have now been synthesized, including ReAsH, a resorufin derivative which is excitable at 590 nm and red fluorescent. These analogous biarsenicals enable affinity chromatography, fluorescence anisotropy measurements, and electron-microscopic localization of tetracysteine-tagged proteins.

Bottom Line: This review is confined to sensors that use fluorescence to transmit biochemical information.Fluorescence is, by far, the most frequently exploited phenomenon for chemical sensors and biosensors.To achieve selective (bio)molecular recognition based on these fluorescence phenomena, various fluorescent elements such as small organic molecules, enzymes, antibodies, and oligonucleotides have been designed and synthesized over the past decades.

View Article: PubMed Central - PubMed

Affiliation: Health Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Central 6, 1-1-1 Higashi, Tsukuba 305-8566, Japan. suzuki-yoshio@aist.go.jp.

ABSTRACT
This review is confined to sensors that use fluorescence to transmit biochemical information. Fluorescence is, by far, the most frequently exploited phenomenon for chemical sensors and biosensors. Parameters that define the application of such sensors include intensity, decay time, anisotropy, quenching efficiency, and luminescence energy transfer. To achieve selective (bio)molecular recognition based on these fluorescence phenomena, various fluorescent elements such as small organic molecules, enzymes, antibodies, and oligonucleotides have been designed and synthesized over the past decades. This review describes the immense variety of fluorescent probes that have been designed for the recognitions of ions, small and large molecules, and their biological applications in terms of intracellular fluorescent imaging techniques.

Show MeSH
Related in: MedlinePlus