Homogeneous assay for biotin based on Aequorea victoria bioluminescence resonance energy transfer system

Gorokhovatsky, Andrey Yu.; Rudenko, N. V.; Marchenkov, Victor V.; Skosyrev, Vitaly S; Arzhanov, Maxim A.; Burkhardt, Nils; Zakharov, M. V.; Semisotnov, Gennady V.; Vinokurov, Leonid M.; Alakhov, Yuli B.

doi:10.1016/s0003-2697(02)00514-6

Cited by 23 publications

(15 citation statements)

References 28 publications

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“…The blue bioluminescence of Aequorin is triggered by Ca 2+ ions; hence, its principal application is as a reporter for Ca 2+ ions 139. 172 Aequorin has been employed as a BRET donor to monitor the interaction between Streptavidin (fused with Aequorin ) and a biotin carboxyl carrier protein (fused with an EGFP acceptor) 173. In a modified BRET assay, the bioluminescence of biotinylated Aequorin was quenched by Dabcyl or QSY‐7‐labeled avidin upon exposure to Ca 2+ ions 174…”

Section: Biological Materialsmentioning

confidence: 99%

Materials for Fluorescence Resonance Energy Transfer Analysis: Beyond Traditional Donor–Acceptor Combinations

Berti²,

2006

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The use of Förster or fluorescence resonance energy transfer (FRET) as a spectroscopic technique has been in practice for over 50 years. A search of ISI Web of Science with just the acronym "FRET" returns more than 2300 citations from various areas such as structural elucidation of biological molecules and their interactions, in vitro assays, in vivo monitoring in cellular research, nucleic acid analysis, signal transduction, light harvesting and metallic nanomaterials. The advent of new classes of fluorophores including nanocrystals, nanoparticles, polymers, and genetically encoded proteins, in conjunction with ever more sophisticated equipment, has been vital in this development. This review gives a critical overview of the major classes of fluorophore materials that may act as donor, acceptor, or both in a FRET configuration. We focus in particular on the benefits and limitations of these materials and their combinations, as well as the available methods of bioconjugation.

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Section: Biological Materialsmentioning

confidence: 99%

Materials for Fluorescence Resonance Energy Transfer Analysis: Beyond Traditional Donor–Acceptor Combinations

Berti²,

2006

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“…Streptavidin-fused aequorin has also been reported for studying the bioluminescence resonance energy transfer between aequorin and enhanced green fluorescent protein. 16) However, no practical results have been reported for the use of streptavidin-fused luciferases and streptavidinfused photoproteins in bioluminescent sandwich immunoassays. In this study, we report the preparation of the highly purified fusion protein of streptavidin to aequorin (STA-AQ) from inclusion bodies expressed in Escherichia coli cells and its application to bioluminescent immunoassays.…”

mentioning

confidence: 99%

Streptavidin-Aequorin Fusion Protein for Bioluminescent Immunoassay

Inouye

Sato

Sasaki

et al. 2011

Bioscience, Biotechnology, and Biochemistry

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“…The plasmid (pETj/SAV-L-Aeq) encoding streptavidin fused with aequorin was prepared and expressed in E. coli cells BL21 (DE3) as described previously [41] with detailed methods of purification of the fusion protein and measuring of its bioluminescence spectrum.…”

Section: Proteinsmentioning

confidence: 99%

Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution

et al. 2020

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The main events in chaperone-assisted protein folding are the binding and ligand-induced release of substrate proteins. Here, we studied the location of denatured proteins previously bound to the GroEL chaperonin resulting from the action of the GroES co-chaperonin in the presence of Mg-ATP. Fluorescein-labeled denatured proteins (α-lactalbumin, lysozyme, serum albumin, and pepsin in the presence of thiol reagents at neutral pH, as well as an early refolding intermediate of malate dehydrogenase) were used to reveal the effect of GroES on their interaction with GroEL. Native electrophoresis has demonstrated that these proteins tend to be released from the GroEL-GroES complex. With the use of biotin- and fluorescein-labeled denatured proteins and streptavidin fused with luciferase aequorin (the so-called streptavidin trap), the presence of denatured proteins in bulk solution after GroES and Mg-ATP addition has been confirmed. The time of GroES-induced dissociation of a denatured protein from the GroEL surface was estimated using the stopped-flow technique and found to be much shorter than the proposed time of the GroEL ATPase cycle.

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Homogeneous assay for biotin based on Aequorea victoria bioluminescence resonance energy transfer system

Cited by 23 publications

References 28 publications

Materials for Fluorescence Resonance Energy Transfer Analysis: Beyond Traditional Donor–Acceptor Combinations

Materials for Fluorescence Resonance Energy Transfer Analysis: Beyond Traditional Donor–Acceptor Combinations

Streptavidin-Aequorin Fusion Protein for Bioluminescent Immunoassay

Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution

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