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ISSN: 1023-5086

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ISSN: 1023-5086

Scientific and technical

Opticheskii Zhurnal

A full-text English translation of the journal is published by Optica Publishing Group under the title “Journal of Optical Technology”

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DOI: 10.17586/1023-5086-2026-93-08-101-109

УДК: 535.372

Fluorescent probe based on intramolecular proton phototransfer for the detection of bovine serum albumin

For Russian citation (Opticheskii Zhurnal):

Мочалов М.О., Парфёнова Е.В., Слюсаренко Н.В., Слюсарева Е.А. Флуоресцентный зонд на основе внутримолекулярного фотопереноса протона для обнаружения бычьего сывороточного альбумина // Оптический журнал. 2026. Т. 93. № 8. С. 101–109. http://doi.org/10.17586/1023-5086-2026-93-08-101-109

Mochalov M. O., Parfenova E. V., Slyusarenko N. V., Slyusareva E. A. Fluorescent probe based on intramolecular proton phototransfer for the detection of bovine serum albumin [in Russian] // Opticheskii Zhurnal. 2026. V. 93. № 8. С. 101–109. http://doi.org/10.17586/1023-5086-2026-93-08-101-109

For citation (Journal of Optical Technology):
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Abstract:

Scope of research. Disodium salt of 3-(1,3-benzothiazol-2-yl)-4-[(2-sulfonatobenzoyl)amino] benzenesulfonic acid, which exhibits ultraviolet-induced double-band luminescence in the visible region of the spectrum. Aim of the study. Testing the hypothesis of sensitivity of the luminescence of the compound to binding to the protein bovine serum albumin. Method. The study was carried out using the methods of steady-state, time-resolved and polarized luminescence. Main results. It was shown that the long-wavelength luminescence band with a large Stokes shift is formed by luminophore conformers capable to phototautomerization. Upon addition of bovine serum albumin, a protein-luminophore complex is formed, leading to an increase in the long-wavelength luminescence intensity. The amplitude ratio of the two luminescence bands can use as an analytical signal for protein detection in a concentration range of up to 50 μM with a maximum accuracy of 1 μM. Practical significance. The advantages of the new fluorescent probe include the stability of its luminescent properties over a wide pH range (3.2–9.9), the absence of heavy atoms in its structure, and the ability to perform quantitative analysis of protein content without an external reference.

Keywords:

fluorescent probe, luminescence, intramolecular proton phototransfer, excited-state intramolecular proton transfer, phototautomerization, bovine serum albumin, double-band luminescence

Acknowledgements:

the work was carried out within the framework of the State Assignment of the Ministry of Education and Science of the Russian Federation, grant FSRZ-2026-0011. The authors express their gratitude to S.V. Kulagin for providing the luminophore, L.A. Sukovatyi for molecular modeling and visualization of the electrostatic potential distribution of the protein surface.

OCIS codes: 300.6280, 300.6390, 170.6280

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