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Lability of Stationary and Time-Resolved Optical Properties of the Conformationally Locked CFP Chromophore Derivative

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Abstract—

The solvatochromic behavior of a model compound mimicking the chromophore of cyan fluorescent protein (CFP) in the spectral and time domains has been studied. Analysis of the time-resolved fluorescence signal, carried out in 40 solvents belonging to different classes, showed that the lipophilic environment promotes an increase, while aromatic solvents and tertiary amines, a decrease in the fluorescence lifetime of the chromophore. Based on this study, the possible rational design of CFP-like proteins was proposed.

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Funding

The study was financed by the Russian Science Foundation (project no. 20-14-00255).

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Correspondence to N. S. Baleeva.

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The article does not contain a description of research carried out by any of the authors of this work involving humans or using animals as objects.

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The authors declare they have no conflict of interest.

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Abbreviations: CFP, cyan fluorescent protein; FQY, fluorescence quantum yield; FP, fluorescent protein.

Corresponding author: phone: +7 (926) 704-13-72.

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Bogdanov, A.M., Gorbachev, D.A., Zaitseva, E.R. et al. Lability of Stationary and Time-Resolved Optical Properties of the Conformationally Locked CFP Chromophore Derivative. Russ J Bioorg Chem 47, 784–787 (2021). https://doi.org/10.1134/S1068162021030043

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  • DOI: https://doi.org/10.1134/S1068162021030043

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