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Ca2+-Regulated Photoproteins: Effective Immunoassay Reporters [Text] / L. A. Frank // Sensors. - 2010. - Vol. 10, Is. 12. - P11287-11300, DOI 10.3390/s101211287. - Cited References: 70. - This work was supported by the grant No. 76 of the Russian Academy of Sciences, Siberian Branch. . - ISSN 1424-8220

РУБ Chemistry, Analytical + Electrochemistry + Instruments & Instrumentation
Рубрики:
POLYMERASE-CHAIN-REACTION
   CYTOKINE MESSENGER-RNA
   BIOLUMINESCENT IMMUNOASSAY
   MYCOBACTERIUM-TUBERCULOSIS
   BIOTINYLATED AEQUORIN
   RECOMBINANT AEQUORIN
   ANGSTROM RESOLUTION
   FUSION PROTEIN
   PCR ASSAY
   OBELIN
Кл.слова (ненормированные):
bioluminescence -- Ca2+-regulated photoprotein -- immunoassay -- PCR-ELISA -- multiplex assay -- re-engineered photoproteins
Аннотация: Ca2+-regulated photoproteins of luminous marine coelenterates are of interest and a challenge for researchers as a unique bioluminescent system and as a promising analytical instrument for both in vivo and in vitro applications. The proteins are comprehensively studied as to biochemical properties, tertiary structures, bioluminescence mechanism, etc. This knowledge, along with available recombinant proteins serves the basis for development of unique bioluminescent detection systems that are "self-contained", triggerable, fast, highly sensitive, and non-hazardous. In the paper, we focus on the use of photoproteins as reporters in binding assays based on immunological recognition element-bioluminescent immunoassay and hybridization immunoassay, their advantages and prospects.

Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.

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Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins / P. V. Natashin [et al.] // FEBS J. - 2014. - Vol. 281, Is. 5. - P1432-1445, DOI 10.1111/febs.12715 . - ISSN 1742-4658
Кл.слова (ненормированные):
aequorin -- bioluminescence -- coelenterazine, obelin -- 6 (4 hydroxyphenyl) derivative -- aequorin -- benzene derivative -- calcium ion -- hydromedusan -- mutant protein -- obelin -- oxygen -- photoprotein -- unclassified drug -- amino acid substitution -- article -- bioluminescence -- calcium transport -- crystal structure -- fluorescence -- hydrogen bond -- priority journal -- protein conformation -- protein structure -- wild type -- Coelenterata -- aequorin -- bioluminescence -- Ca2+-regulated photoprotein -- coelenterazine, obelin -- Amino Acid Substitution -- Animals -- Conserved Sequence -- Crystallography, X-Ray -- Hydrogen Bonding -- Hydrozoa -- Luminescent Proteins -- Models, Molecular -- Mutagenesis, Site-Directed -- Mutant Proteins -- Protein Conformation -- Spectrophotometry
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine coelenterates. All hydromedusan photoproteins are a single-chain polypeptide to which 2- hydroperoxycoelenterazine is tightly but non-covalently bound. Bioluminescence results from oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. The bioluminescence spectral maxima of recombinant photoproteins vary in the range 462-495 nm, despite a high degree of identity of amino acid sequences and spatial structures of these photoproteins. Based on studies of obelin and aequorin mutants with substitution of Phe to Tyr and Tyr to Phe, respectively [Stepanyuk GA et al. (2005) FEBS Lett 579, 1008-1014], it was suggested that the spectral differences may be accounted for by an additional hydrogen bond between the hydroxyl group of a Tyr residue and an oxygen atom of the 6-(p-hydroxyphenyl) substituent of coelenterazine. Here, we report the crystal structures of two conformation states of the F88Y obelin mutant that has bioluminescence and product fluorescence spectra resembling those of aequorin. Comparison of spatial structures of the F88Y obelin conformation states with those of wild-type obelin clearly shows that substitution of Phe to Tyr does not affect the overall structures of either F88Y obelin or its product following Ca2+ discharge, compared to the conformation states of wild-type obelin. The hydrogen bond network in F88Y obelin being due to the Tyr substitution clearly supports the suggestion that different hydrogen bond patterns near the oxygen of the 6-(p-hydroxyphenyl) substituent are the basis for spectral modifications between hydromedusan photoproteins. Comparison of spatial structures and the hydrogen bond network formed into the substrate-binding cavity of WT obelin, F88Y obelin, and aequorin clearly shows that the main cause determining different light emission colors of hydromedusan photoproteins is a different arrangement of the hydrogen-bond network near OH group of 6-(p-hydroxyphenyl) substituent of coelenterazine due to the presence of either Phe or Tyr residue. © 2014 FEBS.

Scopus
Держатели документа:
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Krasnoyarsk 660036, Russian Federation
Laboratory of Bioluminescence Biotechnology, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Russian Federation
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United States
IHuman Institute, ShanghaiTech University, Shanghai, China : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Natashin, P.V.; Markova, S.V.; Lee, J.; Vysotski, E.S.; Liu, Z.-J.

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Application of Enzyme Bioluminescence for Medical Diagnostics [Text] / L. A. Frank, V. V. Krasitskaya // Adv. Biochem. Eng. Biotechnol. : SPRINGER-VERLAG BERLIN, 2014. - Vol. 144. - P175-197. - (Advances in Biochemical Engineering-Biotechnology), DOI 10.1007/978-3-662-43385-0_6. - Cited References:63 . -

РУБ Biotechnology & Applied Microbiology
Рубрики:
RESONANCE ENERGY-TRANSFER
POLYMERASE-CHAIN-REACTION
LUCIFERASE
Кл.слова (ненормированные):
Bioluminescence -- Ca2+-regulated photoprotein -- Diagnostics -- Immunoassay -- Luciferase -- Nucleic acid hybridization assay
Аннотация: Nowadays luciferases are effectively used as analytical instruments in a great variety of research fields. Of special interest are the studies dealing with elaboration of novel analytical systems for the purposes of medical diagnostics. The ever-expanding spectrum of clinically important analytes accounts for the increasing demand for new techniques for their detection. In this chapter we have made an attempt to summarize the results on applications of luciferases as reporters in binding assays including immunoassay, nucleic acid hybridization assay, and so on. The data over the last 15 years have been analyzed and clearly show that luciferase-based assays, due to extremely high sensitivity, low cost, and the lack of need for skilled personnel, hold much promise for clinical diagnostics.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
ИБФ СО РАН

Доп.точки доступа:
Frank, Ludmila A.; Krasitskaya, Vasilisa V.

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Coelenterazine-dependent luciferases as a powerful analytical tool for research and biomedical applications / V. V. Krasitskaya, E. E. Bashmakova, L. A. Frank // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 20. - Ст. 7465. - P1-31, DOI 10.3390/ijms21207465 . - ISSN 1661-6596
Кл.слова (ненормированные):
Analytical systems -- Bioluminescence -- Ca2+-regulated photoprotein -- Coelenterazine -- Luciferase
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate—coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization—Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme–substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
School of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Krasitskaya, V. V.; Bashmakova, E. E.; Frank, L. A.

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