N-extended photoprotein obelin to competitively detect small protein tumor markers.

Autor: Bashmakova EE; Institute of Biophysics SB RAS, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Krasnoyarsk, 660036, Russia., Panamarev NS; Institute of Biophysics SB RAS, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Krasnoyarsk, 660036, Russia; Siberian Federal University, Krasnoyarsk, 660041, Russia., Kudryavtsev AN; Institute of Biophysics SB RAS, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Krasnoyarsk, 660036, Russia., Frank LA; Institute of Biophysics SB RAS, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Krasnoyarsk, 660036, Russia; Siberian Federal University, Krasnoyarsk, 660041, Russia. Electronic address: lfrank@yandex.ru.
Jazyk: angličtina
Zdroj: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2022 Apr 02; Vol. 598, pp. 69-73. Date of Electronic Publication: 2022 Feb 06.
DOI: 10.1016/j.bbrc.2022.02.011
Abstrakt: Two variants of Ca 2+ -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 Ca 2+ -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.
Competing Interests: Declaration of competing interest The authors declare no conflicts of interest.
(Copyright © 2022 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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