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1.
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. -
Vol. 96
,
Is. 5
. - P. 1041-1046,
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. . - 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.
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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, V. V.; Goncharova, N. S.; Biriukov, V. V.; Bashmakova, E. E.; Kabilov, M. R.; Baykov, I. K.; Sokolov, A. Е.; Соколов, Алексей Эдуардович; Frank, L. A.; Russian Foundation for Basic Research (RFBR)Russian Foundation for Basic Research (RFBR) [18-38-00531]
}
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2.
Ultraviolet fluorescence of
coelenteramide and coelenteramide-containing fluorescent proteins. Experimental and theoretical study / R. R. Alieva [et al.]> // J. Photochem. Photobiol. B Biol. - 2016. -
Vol. 162
. - P. 318-323,
DOI
10.1016/j.jphotobiol.2016.07.004. - Cited References: 49. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences (project No 01201351504); the Russian Foundation for Basic Research, Grant No 15-43-04377-sibir; and Russian president's grant NSh-7559.2016.2. . - ISSN 1011-1344
РУБ
Biochemistry & Molecular Biology + Biophysics
Рубрики:
DENSITY-FUNCTIONAL THEORY
ELECTRON-EXCITED-STATES
PHOTOPROTEIN OBELIN
DISCHARGED-OBELIN
LIGHT-EMITTERS
BIOLUMINESCENCE
AEQUORIN
LUMINESCENCE
MECHANISM
CHEMILUMINESCENCE
Кл.слова (ненормированные):
Coelenteramide
--
Fluorescent protein
--
Discharged photoproteins
--
Obelin
--
Aequorin
--
Fluorescence
--
Excitation energy
--
Fluorescence
--
B3LYP
Аннотация:
Coelenteramide-containing fluorescent proteins are products of bioluminescent reactions of marine coelenterates. They are called ‘discharged photoproteins’. Their light-induced fluorescence spectra are variable, depending considerably on external conditions. Current work studies a dependence of light-induced fluorescence spectra of discharged photoproteins obelin, aequorin, and clytin on excitation energy. It was demonstrated that photoexcitation to the upper electron-excited states (260–300 nm) of the discharged photoproteins initiates a fluorescence peak in the near UV region, in addition to the blue-green emission. To characterize the UV fluorescence, the light-induced fluorescence spectra of coelenteramide (CLM), fluorophore of the discharged photoproteins, were studied in methanol solution. Similar to photoproteins, the CLM spectra depended on photoexcitation energy; the additional peak (330 nm) in the near UV region was observed in CLM fluorescence at higher excitation energy (260–300 nm). Quantum chemical calculations by time depending method with B3LYP/cc-pVDZ showed that the conjugated pyrazine-phenolic fragment and benzene moiety of CLM molecule are responsible for the additional UV fluorescence peak. Quantum yields of CLM fluorescence in methanol were 0.028 ± 0.005 at 270–340 nm photoexcitation. A conclusion was made that the UV emission of CLM might contribute to the UV fluorescence of the discharged photoproteins. The study develops knowledge on internal energy transfer in biological structures – complexes of proteins with low-weight aromatic molecules. © 2016 Elsevier B.V.
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Держатели документа:
Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, Russian Federation
Institute of Physics SB RAS, Akademgorodok 50/38, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodny Prospect 79, Krasnoyarsk, Russian Federation
Доп.точки доступа:
Alieva, R. R.; Tomilin, F. N.; Томилин, Феликс Николаевич; Kuzubov, A. A.; Кузубов, Александр Александрович; Ovchinnikov, S. G.; Овчинников, Сергей Геннадьевич; Kudryasheva, N. S.
}
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