Библиотека института биофизики СО РАН

Главная

Базы данных

Труды сотрудников ИБФ СО РАН - результаты поиска

Вид поиска

Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН

Иностранные журналы библиотеки Института биофизики СО РАН

Отечественные журналы библиотеки Института биофизики СО РАН

Каталог диссертаций ИБФ СО РАН

Труды сотрудников ИБФ СО РАН

Область поиска

в найденном

Формат представления найденных документов:
полный	информационный	краткий

Отсортировать найденные документы по:
автору	заглавию	году издания	типу документа

Поисковый запрос: (<.>K=Obelin<.>)

Общее количество найденных документов : 139
Показаны документы с 1 по 20

1-20 21-40 41-60 61-80 81-100 101-120

N-extended photoprotein obelin to competitively detect small protein tumor markers / E. E. Bashmakova, N. S. Panamarev, A. N. Kudryavtsev, L. A. Frank // Biochem. Biophys. Res. Commun. - 2022. - Vol. 598. - P69-73, DOI 10.1016/j.bbrc.2022.02.011. - Cited References:15. - The work was partially supported by a grant of the President of the Russian Federation for young scientists, the candidates of sciences (project MK-772.2020.4, study of a hybrid protein with melanoma-inhibiting activity) and Government of Krasnoyarsk Territory, Krasnoyarsk Regional Science Foundation (project No 2021012006966, study of a hybrid with protein survivin). . - ISSN 0006-291X. - ISSN 1090-2104

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
MELANOMA INHIBITORY-ACTIVITY
SURVIVIN
Кл.слова (ненормированные):
Photoprotein obelin -- Genetic fusion -- Tumor marker -- Competitive assay
Аннотация: Two variants of Ca2+-regulated photoprotein obelin, extended from the N-terminus with small tumor markers-melanoma inhibitory activity protein (MIA) and survivin, one of the protein inhibitors of apoptosis, were designed, obtained and studied. Both domains in the obtained hybrid proteins exhibit the properties of the initial molecules: the main features of Ca2+-triggered bioluminescence are close to those of obelin, and the tumor markers' domains are recognized and bound by the corresponding antibodies. The obtained hybrids compete with the corresponding tumor markers for binding with antibodies, immobilized on the surface and their use has been shown to be promising as bioluminescent labels in a one-stage solid-phase competitive immunoassay. (c) 2022 Published by Elsevier Inc.

WOS
Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Bashmakova, Eugenia E.; Panamarev, Nikita S.; Kudryavtsev, Alexander N.; Frank, Ludmila A.; Kudryavtsev, Alexander; Russian Federation for young scientists [MK-772.2020.4]; Government of Krasnoyarsk Territory, Krasnoyarsk Regional Science Foundation [2021012006966]

Найти похожие

H2O-Bridged Proton-Transfer Channel in Emitter Species Formation in Obelin Bioluminescence / S. F. Chen, E. S. Vysotski, Y. J. Liu // J. Phys. Chem. B. - 2021. - Vol. 125, Is. 37. - P10452-10458, DOI 10.1021/acs.jpcb.1c03985. - Cited References:50. - This work was supported by the Program of Shanghai Institute of Technology (no. YJ2016-42), the National Natural Science Foundation of China (21973005 and 21911530094), and the Russian Foundation for Basic Research (20-04-00085 and 19-14-53004). . - ISSN 1520-6106. - ISSN 1520-5207

РУБ Chemistry, Physical
Рубрики:
CHEMILUMINESCENT DECOMPOSITION
   FLUORESCENCE-SPECTRA
   MECHANISM
   QM/MM
Аннотация: Bioluminescence of a number of marine organisms is conditioned by Ca2+-regulated photoprotein (CaRP) with coelenterazine as the reaction substrate. The reaction product, coelenteramide, at the first singlet excited state (S-1) is the emitter of CaRP. The S-1-state coelenteramide is produced via the decomposition of coelenterazine dioxetanone. Experiments suggested that the neutral S-1-coelenteramide is the primary emitter species. This supposition contradicts with theoretical calculations showing that the anionic S-1-coelenteramide is a primary product of the decomposition of coelenterazine dioxetanone. In this study, applying molecular dynamic (MD) simulations and the hybrid quantum mechanics/molecular mechanics (QM/MM) method, we investigated a proton-transfer (PT) process taking place in CaRP obelin from Obelia longissima for emitter formation. Our calculations demonstrate a concerted PT process with a water molecule as a bridge between anionic S-1-coelenteramide and the nearest histidine residue. The low activation barrier as well as the strong hydrogen-bond network between the proton donor and the proton acceptor suggests a fast PT process comparable with that of the lifetime of excited anionic S-1-coelenteramide. The existence of the PT process eliminates the discrepancy between experimental and theoretical studies. The fast PT process at emitter formation can also take place in other CaRPs.

WOS
Держатели документа:
Shanghai Inst Technol, Sch Chem & Environm Engn, Shanghai 201418, Peoples R China.
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photo Biol Lab, Krasnoyarsk 660036, Russia.
Beijing Normal Univ Zhuhai, Ctr Adv Mat Res, Adv Inst Nat Sci, Zhuhai 519087, Peoples R China.
Beijing Normal Univ, Coll Chem, Key Lab Theoret & Computat Photochem, Minist Educ, Beijing 100875, Peoples R China.

Доп.точки доступа:
Chen, Shu-Feng; Vysotski, Eugene S.; Liu, Ya-Jun; Vysotski, Eugene; Program of Shanghai Institute of Technology [YJ2016-42]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [21973005, 21911530094]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085, 19-14-53004]

Найти похожие

H2O-Bridged Proton-Transfer Channel in Emitter Species Formation in Obelin Bioluminescence / S. -F. Chen, E. S. Vysotski, Y. -J. Liu // J Phys Chem B. - 2021, DOI 10.1021/acs.jpcb.1c03985 . - Article in press. - ISSN 1520-6106
Кл.слова (ненормированные):
Amino acids -- Excited states -- Hydrogen bonds -- Molecular dynamics -- Molecular modeling -- Molecules -- Phosphorescence -- Proton transfer -- Quantum theory -- Fast protons -- Marine organisms -- Photoproteins -- Primary products -- Proton transfer process -- Quantum mechanics/molecular mechanics -- Reaction substrates -- Singlet excited state -- Theoretical calculations -- Transfer channel -- Bioluminescence
Аннотация: Bioluminescence of a number of marine organisms is conditioned by Ca2+-regulated photoprotein (CaRP) with coelenterazine as the reaction substrate. The reaction product, coelenteramide, at the first singlet excited state (S1) is the emitter of CaRP. The S1-state coelenteramide is produced via the decomposition of coelenterazine dioxetanone. Experiments suggested that the neutral S1-coelenteramide is the primary emitter species. This supposition contradicts with theoretical calculations showing that the anionic S1-coelenteramide is a primary product of the decomposition of coelenterazine dioxetanone. In this study, applying molecular dynamic (MD) simulations and the hybrid quantum mechanics/molecular mechanics (QM/MM) method, we investigated a proton-transfer (PT) process taking place in CaRP obelin from Obelia longissima for emitter formation. Our calculations demonstrate a concerted PT process with a water molecule as a bridge between anionic S1-coelenteramide and the nearest histidine residue. The low activation barrier as well as the strong hydrogen-bond network between the proton donor and the proton acceptor suggests a fast PT process comparable with that of the lifetime of excited anionic S1-coelenteramide. The existence of the PT process eliminates the discrepancy between experimental and theoretical studies. The fast PT process at emitter formation can also take place in other CaRPs. © 2021 American Chemical Society.

Scopus
Держатели документа:
School of Chemical and Environmental Engineering, Shanghai Institute of Technology, Shanghai, 201418, China
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center, Krasnoyarsk Science Center SB RAS, Krasnoyarsk, 660036, Russian Federation
Center for Advanced Materials Research, Advanced Institute of Natural Sciences, Beijing Normal University at Zhuhai, Zhuhai, 519087, China
Key Laboratory of Theoretical and Computational Photochemistry, Ministry of Education, College of Chemistry, Beijing Normal University, Beijing, 100875, China

Доп.точки доступа:
Chen, S. -F.; Vysotski, E. S.; Liu, Y. -J.

Найти похожие

Unexpected Coelenterazine Degradation Products of Beroe abyssicola Photoprotein Photoinactivation / L. P. Burakova, M. S. Lyakhovich, K. S. Mineev [et al.] // Org. Lett. - 2021. - Vol. 23, Is. 17. - P6846-6849, DOI 10.1021/acs.orglett.1c02410. - Cited References:20. - This work was supported by grant 20-04-00085 of the Russian Foundation for Basic Research, grant 20-44-242003 of the Russian Foundation for Basic Research, Krasnoyarsk Territory, and Krasnoyarsk Regional Fund of Science in part of purification and spectral characterization of native compounds, grant 17-1401169p of the Russian Science Foundation, and the President of Russian Federation grant for Leading Scientific Schools LS-2605.2020.4 in part of structural elucidation of native products and organic synthesis. We thank Konstantin Antonov (IBCh RAS) and Igor Ivanov (IBCh RAS) for the registration of HRMS spectra. . - ISSN 1523-7060. - ISSN 1523-7052

РУБ Chemistry, Organic
Рубрики:
CRYSTAL-STRUCTURE
   BIOLUMINESCENCE
   OBELIN
   RESIDUES
   BINDING
Аннотация: Ca2+-regulated photoproteins of ctenophores lose bioluminescence activity when exposed to visible light. Little is known about the chemical nature of chromophore photo-inactivation. Using a total synthesis strategy, we have established the structures of two unusual coelenterazine products, isolated from recombinant berovin of the ctenophore Beroe abyssicola, which are Z/E isomers. We propose that during light irradiation, these derivatives are formed from 2-hydroperoxycoelenterazine via the intermediate 8a-peroxide by a mechanism reminiscent of that previously described for the auto-oxidation of green-fluorescent-protein-like chromophores.

WOS
Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photo Biol Lab, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia.
Moscow Inst Phys & Technol, Dolgoprudnyi 141701, Russia.
Pirogov Russian Natl Res Med Univ, Moscow 117997, Russia.

Доп.точки доступа:
Burakova, Ludmila P.; Lyakhovich, Maria S.; Mineev, Konstantin S.; Petushkov, Valentin N.; Zagitova, Renata, I; Tsarkova, Aleksandra S.; Kovalchuk, Sergey, I; Yampolsky, Ilia, V; Vysotski, Eugene S.; Kaskova, Zinaida M.; Mineev, Konstantin; Tsarkova, Aleksandra; Vysotski, Eugene; Kaskova, Zinaida; Burakova, Lyudmila; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085]; Russian Foundation for Basic Research, Krasnoyarsk Territory [20-44-242003]; Krasnoyarsk Regional Fund of Science in part of purification and spectral characterization of native compounds; Russian Science FoundationRussian Science Foundation (RSF) [17-1401169p]; Russian FederationRussian Federation [LS-2605.2020.4]

Найти похожие

Crystal structure of semisynthetic obelin-v / M. D. Larionova, L. J. Wu, E. V. Eremeeva [et al.] // Protein Sci. - 2021, DOI 10.1002/pro.4244. - Cited References:69. - National Natural Science Foundation of China, Grant/Award Number: 32011530076; Russian Foundation for Basic Research, Grant/Award Numbers: 20-04-00085, 20-44-240006, 20-54-53011 . - Article in press. - ISSN 0961-8368. - ISSN 1469-896X

РУБ Biochemistry & Molecular Biology
Рубрики:
CA2+-REGULATED PHOTOPROTEIN OBELIN
PHOTOLUMINESCENCE QUANTUM YIELD
Кл.слова (ненормированные):
analog -- bioluminescence -- coelenterazine -- coelenterazine-v -- obelin -- photoprotein -- protein structure
Аннотация: Coelenterazine-v (CTZ-v), a synthetic derivative with an additional benzyl ring, yields a bright bioluminescence of Renilla luciferase and its "yellow" mutant with a significant shift in the emission spectrum toward longer wavelengths, which makes it the substrate of choice for deep tissue imaging. Although Ca2+-regulated photoproteins activated with CTZ-v also display red-shifted light emission, in contrast to Renilla luciferase their bioluminescence activities are very low, which makes photoproteins activated by CTZ-v unusable for calcium imaging. Here, we report the crystal structure of Ca2+-regulated photoprotein obelin with 2-hydroperoxycoelenterazine-v (obelin-v) at 1.80 angstrom resolution. The structures of obelin-v and obelin bound with native CTZ revealed almost no difference; only the minor rearrangement in hydrogen-bond pattern and slightly increased distances between key active site residues and some atoms of 2-hydroperoxycoelenterazine-v were found. The fluorescence quantum yield (phi(FL)) of obelin bound with coelenteramide-v (0.24) turned out to be even higher than that of obelin with native coelenteramide (0.19). Since both obelins are in effect the enzyme-substrate complexes containing the 2-hydroperoxy adduct of CTZ-v or CTZ, we reasonably assume the chemical reaction mechanisms and the yields of the reaction products (phi(R)) to be similar for both obelins. Based on these findings we suggest that low bioluminescence activity of obelin-v is caused by the low efficiency of generating an electronic excited state (phi(S)). In turn, the low phi(S) value as compared to that of native CTZ might be the result of small changes in the substrate microenvironment in the obelin-v active site.

WOS
Держатели документа:
SB RAS, Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Photobiol Lab, Inst Biophys, Krasnoyarsk, Russia.
ShanghaiTech Univ, iHuman Inst, Ren Bldg,393 Middle Huaxia Rd, Shanghai 201210, Peoples R China.
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Krasnoyarsk, Russia.
ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai, Peoples R China.

Доп.точки доступа:
Larionova, Marina D.; Wu, Lijie; Eremeeva, Elena, V; Natashin, Pavel, V; Gulnov, Dmitry, V; Nemtseva, Elena, V; Liu, Dongsheng; Liu, Zhi-Jie; Vysotski, Eugene S.; Eremeeva, Elena; Nemtseva, Elena; Vysotski, Eugene; Gulnov, Dmitry; Natashin, Pavel; Larionova, Marina; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [32011530076]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085, 20-44-240006, 20-54-53011]

Найти похожие

The Ca2+-Regulated Photoprotein Obelin as a Tool for SELEX Monitoring and DNA Aptamer Affinity Evaluation / V. V. Krasitskaya, N. S. Goncharova, V. V. Biriukov [et al.] // Photochem. Photobiol. - 2020, DOI 10.1111/php.13274. - Cited References:25. - This work has been supported by the Russian Foundation for Basic Research (RFBR) under the grant no 18-38-00531. . - Article in press. - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CARDIAC TROPONIN-I
   BIOLUMINESCENCE
   IMMUNOASSAY
   APTASENSOR
   DIAGNOSIS
Аннотация: Bioluminescent solid-phase analysis was proposed to monitor the selection process and to determine binding characteristics of the aptamer-target complexes during design and development of the specific aptamers. The assay involves Ca2+-regulated photoprotein obelin as a simple, sensitive and fast reporter. Applicability and the prospects of the approach were exemplified by identification of DNA aptamers to cardiac troponin I, a highly specific early biomarker for acute myocardial infarction. Two structurally different aptamers specific to various epitopes of troponin I were obtained and then tested in a model bioluminescent assay.

WOS
Держатели документа:
Fed Res Ctr KSC SB RAS, Inst Biophys SB RAS, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
Inst Chem Biol & Fundamental Med SB RAS, Novosibirsk, Russia.
Fed Res Ctr KSC SB RAS, Kirensky Inst Phys, Krasnoyarsk, Russia.

Доп.точки доступа:
Krasitskaya, Vasilisa V.; Goncharova, Natalia S.; Biriukov, Vladislav V.; Bashmakova, Eugenia E.; Kabilov, Marsel R.; Baykov, Ivan K.; Sokolov, Aleksey E.; Frank, Ludmila A.; Russian Foundation for Basic Research (RFBR)Russian Foundation for Basic Research (RFBR) [18-38-00531]

Найти похожие

Luminescence Activity Decreases Whenv-coelenterazine Replaces Coelenterazine in Calcium-Regulated Photoprotein-A Theoretical and Experimental Study / B. W. Ding, E. V. Eremeeva, E. S. Vysotski, Y. J. Liu // Photochem. Photobiol. - 2020, DOI 10.1111/php.13280. - Cited References:68. - This study was sponsored by the National Natural Science Foundation of China (Grant No. 21911530094, 21673020 and 21973005) and RFBR (Grant No. 19-54-53004 and 20-54-53011). Ding also thank the support from the China Postdoctoral Science Foundation (Grant No. 2018M630100). . - Article in press. - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
RECOMBINANT SEMISYNTHETIC AEQUORINS
OBELIN BIOLUMINESCENCE
MECHANISTIC
Аннотация: Calcium-regulated photoproteins are found in at least five phyla of organisms. The light emitted by those photoproteins can be tuned by mutating the photoprotein and/or by modifying the substrate coelenterazine (CTZ). Thirty years ago, Shimomura observed that the luminescence activity of aequorin was dramatically reduced when the substrate CTZ was replaced by its analogv-CTZ. The latter is formed by adding a phenyl ring to the pi-conjugated moiety of CTZ. The decrease in luminescence activity has not been understood until now. In this paper, through combined quantum mechanics and molecular mechanics calculations as well as molecular dynamics simulations, we discovered the reason for this observation. Modification of the substrate changes the conformation of nearby aromatic residues and enhances the pi-pi stacking interactions between the conjugated moiety ofv-CTZ and the residues, which weakens the charge transfer to form light emitter and leads to a lower luminescence activity. The microenvironments of CTZ in obelin and in aequorin are very similar, so we predicted that the luminescence activity of obelin will also dramatically decrease when CTZ is replaced byv-CTZ. This prediction has received strong evidence from currently theoretical calculations and has been verified by experiments.

WOS
Держатели документа:
Beijing Normal Univ, Coll Chem, Key Lab Theoret & Computat Photochem, Minist Educ, Beijing, Peoples R China.
RAS, Photobiol Lab, Inst Biophys, SB,Fed Res Ctr,Krasnoyarsk Sci Ctr, Krasnoyarsk, Russia.

Доп.точки доступа:
Ding, Bo-Wen; Eremeeva, Elena V.; Vysotski, Eugene S.; Liu, Ya-Jun; Vysotski, Eugene; National Natural Science Foundation of ChinaNational Natural Science Foundation of China [21911530094, 21673020, 21973005]; RFBRRussian Foundation for Basic Research (RFBR) [19-54-53004, 20-54-53011]; China Postdoctoral Science FoundationChina Postdoctoral Science Foundation [2018M630100]

Найти похожие

Enzymatic Responses to Low-Intensity Radiation of Tritium / T. V. Rozhko, E. V. Nemtseva, M. V. Gardt [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 22. - Ст. 8464, DOI 10.3390/ijms21228464. - Cited References:59. - This work was supported by RFBR-Krasnoyarsk Regional Foundation N 18-44-240004, 18-44-242002. . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
LUMINOUS MARINE-BACTERIA
IONIZING-RADIATION
DISCHARGED-OBELIN
Кл.слова (ненормированные):
hormesis -- low-dose radiation -- tritium -- enzymes -- bacterial luciferase -- oxidoreductase -- fluorescent protein
Аннотация: The present study considers a possible role of enzymatic reactions in the adaptive response of cells to the beta-emitting radionuclide tritium under conditions of low-dose exposures. Effects of tritiated water (HTO) on the reactions of bacterial luciferase and NAD(P)H:FMN-oxidoreductase, as well as a coupled system of these two reactions, were studied at radioactivity concentrations <= 200 MBq/L. Additionally, one of the simplest enzymatic reactions, photobiochemical proton transfer in Coelenteramide-containing Fluorescent Protein (CLM-FP), was also investigated. We found that HTO increased the activity of NAD(P)H:FMN-oxidoreductase at the initial stage of its reaction (by up to 230%); however, a rise of luciferase activity was moderate (<20%). The CLM-FP samples did not show any increase in the rate of the photobiochemical proton transfer under the exposure to HTO. The responses of the enzyme systems were compared to the 'hormetic' response of luminous marine bacterial cells studied earlier. We conclude that (1) the oxidoreductase reaction contributes significantly to the activation of the coupled enzyme system and bacterial cells by tritium, and (2) an increase in the organization level of biological systems promotes the hormesis phenomenon.

WOS
Держатели документа:
Krasnoyarsk State Med Acad, Dept Med & Biol Phys, Krasnoyarsk 660022, Russia.
Siberian Fed Univ, Biophys Dept, Krasnoyarsk 660041, Russia.
RAS, Inst Biophys, SB, FRC,KSC, Krasnoyarsk 660036, Russia.
Moscow MV Lomonosov State Univ, Dept Chem, Moscow 119991, Russia.

Доп.точки доступа:
Rozhko, Tatiana V.; Nemtseva, Elena V.; Gardt, Maria V.; Raikov, Alexander V.; Lisitsa, Albert E.; Badun, Gennadii A.; Kudryasheva, Nadezhda S.; Nemtseva, Elena; Kudryasheva, Nadezhda; Rozko, Tat'ana; Lisitsa, Albert; RFBR-Krasnoyarsk Regional Foundation [N 18-44-240004, 18-44-242002]

Найти похожие

The Hybrid Protein ZZ-OL as an Analytical Tool for Biotechnology Research / V. V. Krasitskaya, E. E. Bashmakova, A. N. Kudryavtsev [et al.] // Russ. J. Bioorg. Chem. - 2020. - Vol. 46, Is. 6. - P1004-1010, DOI 10.1134/S106816202006014X. - Cited References:14. - The study was partially supported by a grant of the President of the Russian Federation for Young Scientists, the Candidates of Sciences (project MK-772.2020.4 in the part involving the synthesis and analysis of variants of proteins with melanoma-inhibiting activity) and a grant of the Russian Science Foundation (project no. 16-14-10296 in the part involving the bioluminescence analysis of binding of DNA aptamers to targets). . - ISSN 1068-1620. - ISSN 1608-330X

РУБ Biochemistry & Molecular Biology + Chemistry, Organic

Кл.слова (ненормированные):
С -- а -- (2+)-regulated photoprotein obelin -- proZZ -- hybrid -- protein -- IgG -- bioluminescence assay
Аннотация: The gene of the hybrid protein that encodes the double synthetic fragment proZZ of the immunoglobulin-binding domain of protein A of Staphylococcus aureus and apo-obelin joined by a short linker has been cloned. The corresponding hybrid protein has been obtained by expression in Escherichia coli cells. The protein activated with a substrate (coelenterazine) possesses the bioluminescent Ca2+-dependent activity of the photoprotein close to that of recombinant wild-type obelin, and the immunoglobulin-binding ability of protein A. It has been shown that the hybrid can be used as a highly sensitive label to detect antibodies and estimate their affinity and interaction with recombinant proteins, as well as in investigations of other kinds.

WOS
Держатели документа:
Russian Acad Sci, Fed Res Ctr, Krasnoyarsk Res Ctr, Siberian Branch,Inst Biophys, Akad Gorodok 50-50, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Inst Chem Biol & Fundamental Med, Siberian Branch, Novosibirsk 630090, Russia.

Доп.точки доступа:
Krasitskaya, V. V.; Bashmakova, E. E.; Kudryavtsev, A. N.; Vorobjeva, M. A.; Shatunova, E. A.; Frank, L. A.; Russian FederationRussian Federation [MK-772.2020.4]; Russian Science FoundationRussian Science Foundation (RSF) [16-14-10296]

Найти похожие

10.

Luminescence Activity Decreases When v-coelenterazine Replaces Coelenterazine in Calcium-Regulated Photoprotein—A Theoretical and Experimental Study / B. -W. Ding, E. V. Eremeeva, E. S. Vysotski, Y. -J. Liu // Photochem. Photobiol. - 2020, DOI 10.1111/php.13280 . - Article in press. - ISSN 0031-8655
Аннотация: Calcium-regulated photoproteins are found in at least five phyla of organisms. The light emitted by those photoproteins can be tuned by mutating the photoprotein and/or by modifying the substrate coelenterazine (CTZ). Thirty years ago, Shimomura observed that the luminescence activity of aequorin was dramatically reduced when the substrate CTZ was replaced by its analog v-CTZ. The latter is formed by adding a phenyl ring to the ?-conjugated moiety of CTZ. The decrease in luminescence activity has not been understood until now. In this paper, through combined quantum mechanics and molecular mechanics calculations as well as molecular dynamics simulations, we discovered the reason for this observation. Modification of the substrate changes the conformation of nearby aromatic residues and enhances the ?-? stacking interactions between the conjugated moiety of v-CTZ and the residues, which weakens the charge transfer to form light emitter and leads to a lower luminescence activity. The microenvironments of CTZ in obelin and in aequorin are very similar, so we predicted that the luminescence activity of obelin will also dramatically decrease when CTZ is replaced by v-CTZ. This prediction has received strong evidence from currently theoretical calculations and has been verified by experiments. © 2020 American Society for Photobiology

Scopus
Держатели документа:
Key Laboratory of Theoretical and Computational Photochemistry, Ministry of Education, College of Chemistry, Beijing Normal University, Beijing, China
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Ding, B. -W.; Eremeeva, E. V.; Vysotski, E. S.; Liu, Y. -J.

Найти похожие

11.

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, DOI 10.3390/ijms21207465. - Cited References:251. - The work was supported by the Russian State funded budget project of IBP SB RAS No. AAAA-A19-119031890015-0. . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
PROTEIN-PROTEIN INTERACTIONS
CA2+-REGULATED PHOTOPROTEIN OBELIN
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- luciferase -- Ca2+-regulated -- photoprotein -- analytical systems
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.

WOS
Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Sch Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Krasitskaya, Vasilisa V.; Bashmakova, Eugenia E.; Frank, Ludmila A.; Russian State funded budget project of IBP SB RAS [AAAA-A19-119031890015-0]

Найти похожие

12.

13.

Reporter-recruiting bifunctional aptasensor for bioluminescent analytical assays / A. Davydova, V. Krasitskaya, P. Vorobjev [et al.] // RSC Adv. - 2020. - Vol. 10, Is. 54. - P32393-32399, DOI 10.1039/d0ra05117a. - Cited References:33. - The work was supported by the Russian Science Foundation (grant #16-14-10296), Russian State funded budget projects #AAAA-A17-117020210021-7 to ICBFM SB RAS and #AAAA-A19-119031890015-0 to IBP SB RAS. . - ISSN 2046-2069

РУБ Chemistry, Multidisciplinary
Рубрики:
DNA APTAMER
   RNA APTAMER
   OBELIN
   PURIFICATION
   EXPRESSION
   SEQUENCES
Аннотация: We report a novel bioluminescent aptasensor, which consists of 2 '-F-RNA aptamer modules joined into a bi-specific aptamer construct. One aptamer module binds the analyte, then after structural rearrangement the second module recruits non-covalently Ca2+-dependent photoprotein obelin from the solution, thus providing a bioluminescent signal. This concept allows using free protein as a reporter, which brings such advantages as no need for aptamer-protein conjugation, a possibility of thermal re-folding of aptamer component with no harm to a protein, and simpler detection protocol. We developed the new 2 '-F-RNA aptamer for obelin, and proposed the strategy for engineering structure-switching bi-modular aptamer constructs which bind the analyte and the obelin in a sequential manner. With the use of hemoglobin as a model analyte, we showed the feasibility of utilizing the aptasensor in a fast and straightforward bioluminescent microplate assay. With a proper design of a secondary structure, this strategy of aptasensor engineering might be further extended to bi-specific aptamer-based bioluminescent sensors for other analytes of interest.

WOS
Держатели документа:
SB RAS, Inst Chem Biol & Fundamental Med, Novosibirsk 630090, Russia.
SB RAS, Inst Biophys, Fed Res Ctr, Krasnoyarsk Sci Ctr, Krasnoyarsk 660036, Russia.
Novosibirsk State Univ, Pimgova St 2, Novosibirsk 630090, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Davydova, Anna; Krasitskaya, Vasilisa; Vorobjev, Pavel; Timoshenko, Valentina; Tupikin, Alexey; Kabilov, Marsel; Frank, Ludmila; Venyaminova, Alya; Vorobyeva, Mariya; Russian Science FoundationRussian Science Foundation (RSF) [16-14-10296]; Russian State funded budget projects [AAAA-A17-117020210021-7, AAAA-A19-119031890015-0]

Найти похожие

14.

Bioluminescent properties of semi-synthetic obelin and aequorin activated by coelenterazine analogues with modifications of C-2, C-6, and C-8 substituents / E. V. Eremeeva, T. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446. - P1-21, DOI 10.3390/ijms21155446 . - ISSN 1661-6596
Кл.слова (ненормированные):
Aequorin -- Analogues -- Coelenterazine -- Obelin -- Photoprotein
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
Key Laboratory of Chemical Biology (MOE), Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, Jinan, Shandong 250012, China
State Key Laboratory of Microbial Technology, Shandong University–Helmholtz Institute of Biotechnology, Shandong University, Qingdao, Shandong 266237, China

Доп.точки доступа:
Eremeeva, E. V.; Jiang, T.; Malikova, N. P.; Li, M.; Vysotski, E. S.

Найти похожие

15.

Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents / E. V. Eremeeva, T. Y. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446, DOI 10.3390/ijms21155446. - Cited References:50. - The reported study was funded by RFBR and NSFC according to the research project No. 20-54-53011 (E.V.E. and N.P.M.), Russian Foundation for Basic Research (No. 18-44-242001), Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science (E.S.V.), the National Natural Science Foundation of China (No. 81874308), and the Shandong Natural Science Foundation (No. ZR2018ZC0233) (M.L.). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
SPECTROSCOPIC PROPERTIES
Кл.слова (ненормированные):
photoprotein -- obelin -- aequorin -- coelenterazine -- analogues
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues.

WOS
Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photobiol Lab, Fed Res Ctr, Krasnoyarsk 660036, Russia.
Shandong Univ, Sch Pharmaceut Sci, Dept Med Chem, Key Lab Chem Biol MOE, Jinan 250012, Peoples R China.
Shandong Univ, Helmholtz Inst Biotechnol, State Key Lab Microbial Technol, Qingdao 266237, Peoples R China.

Доп.точки доступа:
Eremeeva, Elena, V; Jiang, Tianyu; Malikova, Natalia P.; Li, Minyong; Vysotski, Eugene S.; RFBRRussian Foundation for Basic Research (RFBR); NSFCNational Natural Science Foundation of China (NSFC) [20-54-53011]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-44-242001]; Krasnoyarsk Regional Fund of Science; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [81874308]; Shandong Natural Science FoundationNatural Science Foundation of Shandong Province [ZR2018ZC0233]; Government of Krasnoyarsk Territory

Найти похожие

16.

Exploring Bioluminescence Function of the Ca2+-regulated Photoproteins with Site-directed Mutagenesis / E. V. Eremeeva, E. S. Vysotski // Photochem. Photobiol. - 2019. - Vol. 95, Is. 1. - P8-23, DOI 10.1111/php.12945. - Cited References:88. - This work was supported by grant 17-04-00764 of Russian Foundation for Basic Research and the state budgetallocated to the fundamental research at the Russian Academy of Sciences (project 0356-2017-0017). . - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CALCIUM-BINDING PHOTOPROTEIN
GREEN-FLUORESCENT PROTEIN
JELLYFISH
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- aequorin -- obelin -- clytin -- mitrocomin -- EF-hand protein
Аннотация: Site-directed mutagenesis is a powerful tool to investigate the structure-function relationship of proteins and a function of certain amino acid residues in catalytic conversion of substrates during enzymatic reactions. Hence, it is not surprising that this approach was repeatedly applied to elucidate the role of certain amino acid residues in various aspects of photoprotein bioluminescence, mostly for aequorin and obelin, and to design mutant photoproteins with altered properties (modified calcium affinity, faster or slower bioluminescence kinetics, different emission color) which would either allow the development of novel bioluminescent assays or improvement of characteristics of the already existing ones. This information, however, is scattered over different articles. In this review, we systematize the findings that were made using site-directed mutagenesis studies regarding the impact of various amino acid residues on bioluminescence of hydromedusan Ca2+-regulated photoproteins. All key residues that have been identified are pinpointed, and their influence on different aspects of photoprotein functioning such as active photoprotein complex formation, bioluminescence reaction, calcium response and light emitter formation is discussed.

WOS,
Смотреть статью
Держатели документа:
RAS, SB, Inst Biophys, Fed Res Ctr,Krasnoyarsk Sci Ctr,Photobiol Lab, Krasnoyarsk, Russia.

Доп.точки доступа:
Eremeeva, Elena V.; Vysotski, Eugene S.; Russian Foundation for Basic Research [17-04-00764]; Russian Academy of Sciences [0356-2017-0017]

Найти похожие

17.

Bioluminescent aptamer-based solid-phase microassay to detect lung tumor cells in plasma / E. E. Bashmakova [et al.] // Talanta. - 2019. - Vol. 199. - P674-678, DOI 10.1016/j.talanta.2019.03.030. - Cited References:19. - The authors are grateful to the staff of Krasnoyarsk regional clinical oncology center named after A.I. Kryzhanovsky and particularly doctor Alexey V. Krat for the experimental material provided. This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences, project No. 0356-2017-0017. . - ISSN 0039-9140. - ISSN 1873-3573

РУБ Chemistry, Analytical
Рубрики:
CONJUGATED NANOPARTICLES
   CANCER
   COLLECTION
   LIGANDS
   PROBES
Кл.слова (ненормированные):
DNA aptamers -- Lung tumor -- Bioluminescent solid-phase microassay
Аннотация: Two high-affinity DNA aptamers for lung tumor cells were applied as biospecific elements in bioluminescent assay of patient blood. The oligonucleotide complementary to the 5' end of both aptamers carrying either biotin or Ca2+-regulated photoprotein obelin was used to form a sandwich-type analytical complex on the surfaces of magnetic streptavidin-activated microspherical particles. Clinical blood samples from cases of morphologically confirmed lung cancer and control samples were analyzed applying the developed assay. From the receiver operator curve (ROC) analysis, the chosen threshold value as clinical decision limit offers the sensitivity of 91.5% and the specificity of 75% (p < 0.001). The area under ROC curve with the value of 0.901 distinguishes well between the two groups under investigation.

WOS,
Смотреть статью,
Scopus
Держатели документа:
RAS, Krasnoyarsk Sci Ctr SB, Fed Res Ctr, Inst Biophys SB, Akademgorodok 50-50, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Svobodny Pr 79, Krasnoyarsk 660041, Russia.
State Med Univ, Partizana Zheleznyaka St 1, Krasnoyarsk 660022, Russia.

Доп.точки доступа:
Bashmakova, Eugenia E.; Krasitskaya, Vasilisa V.; Zamay, Galina S.; Zamay, Tatiana N.; Frank, Ludmila A.; Russian Academy of Sciences [0356-2017-0017]

Найти похожие

18.

Bioluminescent aptamer-based sandwich-type assay of anti-myelin basic protein autoantibodies associated with multiple sclerosis / V. V. Krasitskaya [et al.] // Anal. Chim. Acta. - 2019. - Vol. 1064. - P112-118, DOI 10.1016/j.aca.2019.03.015. - Cited References:29. - This work was supported by the Russian Foundation for Basic Research (RFBR), Russia, under the grant No 17-315-50027; Russian State funded budget projects No. AAAA-A17-117013050026-4 and AAAA-A17-117020210021-7. . - ISSN 0003-2670. - ISSN 1873-4324

РУБ Chemistry, Analytical
Рубрики:
ANTIBODIES
BIOMARKERS
RNA
Кл.слова (ненормированные):
Bioluminescent microassay -- RNA aptamers -- Autoantibodies to myelin basic -- protein -- Multiple sclerosis
Аннотация: Bioluminescent solid-phase sandwich-type microassay was developed to detect multiple sclerosis (MS)-associated autoantibodies in human sera. The assay is based on two different 2'-F-Py RNA aptamers against the target autoantibodies as biospecific elements, and Ca2+-regulated photoprotein obelin as a reporter. The paper describes elaboration of the assay and its application to 91 serum samples from patients with clinically definite MS and 86 ones from individuals healthy in terms of MS. Based on the receiver-operator curve (ROC) analysis, the chosen threshold value as clinical decision limit offers sensitivity of 63.7% and specificity of 94.2%. The area under the ROC curve (AUC) value of 0.87 shows a good difference between the groups under investigation. The likelihood ratio of 10.97 proves the diagnostic value of the assay and its potential as one of the laboratory MS-tests. (C) 2019 Elsevier B.V. All rights reserved.

WOS,
Смотреть статью,
Scopus
Держатели документа:
RAS, Krasnoyarsk Sci Ctr SB, Fed Res Ctr, Inst Biophys SB, Krasnoyarsk 660036, Russia.
RAS, Inst Chem Biol & Fundamental Med SB, Novosibirsk 630090, Russia.
State Med Univ, Krasnoyarsk 660022, Russia.

Доп.точки доступа:
Krasitskaya, Vasilisa V.; Chaukina, Valentina V.; Abroskina, Maria V.; Vorobyeva, Maria A.; Ilminskaya, Aleksandra A.; Kabilov, Marsel R.; Prokopenko, Semyon V.; Nevinsky, Georgy A.; Venyaminova, Alya G.; Frank, Ludmila A.; Russian Foundation for Basic Research (RFBR), Russia [17-315-50027]; Russian State [AAAA-A17-117013050026-4, AAAA-A17-117020210021-7]

Найти похожие

19.

Protein-based fluorescent bioassay for low-dose gamma radiation exposures / A. S. Petrova [et al.] // Anal. Bioanal. Chem. - 2018, DOI 10.1007/s00216-018-1282-5 . - ISSN 1618-2642
Кл.слова (ненормированные):
Bioassay -- Enzymes -- Fluorescence/luminescence -- Fluorescent protein -- Gamma radiation -- Radiotoxicity -- Efficiency -- Enzymes -- Fluorescence -- Gamma rays -- Proteins -- Proton transfer -- Fluorescence characteristics -- Fluorescence intensities -- Fluorescence spectra -- Fluorescence/luminescence -- Fluorescent protein -- Photochemical process -- Physiological liquids -- Radiotoxicity -- Bioassay
Аннотация: The study suggests an application of a coelenteramide-containing fluorescent protein (CLM-CFP) as a simplest bioassay for gamma radiation exposures. “Discharged obelin,” a product of the bioluminescence reaction of the marine coelenterate Obelia longissima, was used as a representative of the CLM-CFP group. The bioassay is based on a simple enzymatic reaction—photochemical proton transfer in the coelenteramide-apoprotein complex. Components of this reaction differ in fluorescence color, providing, by this, an evaluation of the proton transfer efficiency in the photochemical process. This efficiency depends on the microenvironment of the coelenteramide within the protein complex, and, hence, can evaluate a destructive ability of gamma radiation. The CLM-CFP samples were exposed to gamma radiation (137Cs, 2 mGy/h) for 7 and 16 days at 20 °C and 5 °C, respectively. As a result, two fluorescence characteristics (overall fluorescence intensity and contributions of color components to the fluorescence spectra) were identified as bioassay parameters. Both parameters demonstrated high sensitivity of the CLM-CFP-based bioassay to the low-dose gamma radiation exposure (up to 100 mGy). Higher temperature (20 °C) enhanced the response of CLM-CFP to gamma radiation. This new bioassay can provide fluorescent multicolor assessment of protein destruction in cells and physiological liquids under exposure to low doses of gamma radiation. [Figure not available: see fulltext.]. © 2018, Springer-Verlag GmbH Germany, part of Springer Nature.

Scopus,
Смотреть статью,
WOS
Держатели документа:
Krasnoyarsk State Agrarian University, Mira Avenue 90, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodnyy Ave 79, Krasnoyarsk, Russian Federation
Institute of Biophysics SB RAS, FRC KSC SB RAS, Krasnoyarsk, Russian Federation
Department of Radiology, University of Pennsylvania, 3401 N Broad St., Philadelphia, PA, United States

Доп.точки доступа:
Petrova, A. S.; Lukonina, A. A.; Dementyev, D. V.; Bolsunovsky, A. Ya. ; Popov, A. V.; Kudryasheva, N. S.

Найти похожие

20.

The Ca2+-Regulated Photoprotein Obelin as a Target for the RNA Aptamer Selection / V. V. Krasitskaya [et al.] // Russ. J. Bioorg. Chem. - 2018. - Vol. 44, Is. 3. - P296-301, DOI 10.1134/S1068162018030093 . - ISSN 1068-1620
Кл.слова (ненормированные):
2'-fluoro-RNA -- in vitro selection -- RNA aptamers -- Са2+-regulated photoprotein obelin
Аннотация: A variant of the Ca2+-regulated photoprotein obelin elongated with a hexahistidine peptide from the N-terminus was developed and studied. After immobilization on a metal-affine sorbent, the hybrid protein was applied as a target for the in vitro selection of RNA aptamers. According to the data of bioluminescent solid-phase microanalysis, the selection was shown to enrich the RNA library with obelin-affine molecules. © 2018, Pleiades Publishing, Ltd.

Scopus,
Смотреть статью,
WOS
Держатели документа:
Institute of Biophysics Siberian Branch, Russian Academy of Sciences, FRC Krasnoyarsk Science Center, Krasnoyarsk, Russian Federation
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences, Novosibirsk, Russian Federation

Доп.точки доступа:
Krasitskaya, V. V.; Davydova, A. S.; Vorobjeva, M. A.; Frank, L. A.

Найти похожие