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Infrared fluorescent protein iRFP as an acceptor for resonance excitation energy transfer

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Abstract

The possibility of bacteriochrome-based infrared fluorescent protein iRFP use as an acceptor for the Förster resonance energy transfer (FRET) was investigated. GFP-like far-red fluorescent proteins mKate2, eqFP650, and eqFP670 were used as energy donors. Bacterial expression vectors encoding donor and acceptor proteins joined by a heptadecapeptide linker were constructed with the goal to test FRET. The efficiency of FRET was estimated in vitro for the isolated proteins from the increase of the donor emission following cleavage of the linker. Among the three tested constructs the eqFP650-iRFP pair demonstrated the most efficient energy transfer (approximately 30%).

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Abbreviations

GFP:

green fluorescent protein

FRET:

Forster (or fluorescence) resonance energy transfer

iRFP:

infrared fluorescent protein

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Authors and Affiliations

  1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia

    O. A. Zlobovskaya, K. S. Sarkisyan & K. A. Lukyanov

  2. Scientific-Research Institute of Biomedical Technologies, Nizhni Novgorod State Medical Academy, pl. Minina 10/1, Nizhni Novgorod, 603005, Russia

    K. A. Lukyanov

Authors
  1. O. A. Zlobovskaya
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  2. K. S. Sarkisyan
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  3. K. A. Lukyanov
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Correspondence to K. A. Lukyanov.

Additional information

Original Russian Text © O.A. Zlobovskaya, K.S. Sarkisyan, K.A. Lukyanov, 2015, published in Bioorganicheskaya Khimiya, 2015, Vol. 41, No. 3, pp. 299–304.

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Zlobovskaya, O.A., Sarkisyan, K.S. & Lukyanov, K.A. Infrared fluorescent protein iRFP as an acceptor for resonance excitation energy transfer. Russ J Bioorg Chem 41, 266–270 (2015). https://doi.org/10.1134/S1068162015030139

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  • DOI: https://doi.org/10.1134/S1068162015030139

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