Bright and stable near-infrared fluorescent protein for in vivo imaging

Grigory S. Filonov; Kiryl D. Piatkevich; Li Min Ting; Jinghang Zhang; Kami Kim; Vladislav V. Verkhusha

doi:10.1038/nbt.1918

Bright and stable near-infrared fluorescent protein for in vivo imaging

Grigory S. Filonov
, Kiryl D. Piatkevich
, Li Min Ting
, Jinghang Zhang
, Kami Kim
, Vladislav V. Verkhusha

Research output: Contribution to journal › Article › peer-review

621 Scopus citations

Abstract

Imaging biological processes in mammalian tissues will be facilitated by fluorescent probes with excitation and emission bands within the near-infrared optical window of high transparency. Here we report a phytochrome-based near-infrared fluorescent protein (iRFP) with excitation and emission maxima at 690 nm and 713 nm, respectively. iRFP does not require an exogenous supply of the chromophore biliverdin and has higher effective brightness, intracellular stability and photostability than earlier phytochrome-derived fluorescent probes. Compared with far-red GFP-like proteins, iRFP has a substantially higher signal-to-background ratio in a mouse model due to its infrared-shifted spectra.

Original language	English (US)
Pages (from-to)	757-761
Number of pages	5
Journal	Nature Biotechnology
Volume	29
Issue number	8
DOIs	https://doi.org/10.1038/nbt.1918
State	Published - Aug 2011

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology
Molecular Medicine
Biomedical Engineering

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10.1038/nbt.1918

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@article{e6965bba6a2b4396b860254d20544ec3,

title = "Bright and stable near-infrared fluorescent protein for in vivo imaging",

abstract = "Imaging biological processes in mammalian tissues will be facilitated by fluorescent probes with excitation and emission bands within the near-infrared optical window of high transparency. Here we report a phytochrome-based near-infrared fluorescent protein (iRFP) with excitation and emission maxima at 690 nm and 713 nm, respectively. iRFP does not require an exogenous supply of the chromophore biliverdin and has higher effective brightness, intracellular stability and photostability than earlier phytochrome-derived fluorescent probes. Compared with far-red GFP-like proteins, iRFP has a substantially higher signal-to-background ratio in a mouse model due to its infrared-shifted spectra.",

author = "Filonov, \{Grigory S.\} and Piatkevich, \{Kiryl D.\} and Ting, \{Li Min\} and Jinghang Zhang and Kami Kim and Verkhusha, \{Vladislav V.\}",

note = "Funding Information: We thank E. Giraud (Institute for Research and Development, France) for the plasmid encoding bacteriophytochrome from R. palustris, A. Ulijasz and R. Vierstra (both from University of Wisconsin) for the plasmid encoding the heme-oxygenase from Synechocystis sp. PCC6803 and B. Glick (University of Chicago), D. Chudakov and K. Lukyanov (both from Institute of Bioorganic Chemistry, Russia) for the plasmids encoding GFP-like far-red fluorescent proteins. We are grateful to D. Entenberg for the help with two-photon excitation measurements, A. Muesch and D. Cohen for the assistance with virus purification and providing GFP-encoding adenoviruses and R. Zheng for the help with size-exclusion chromatography (all from Albert Einstein College of Medicine). This work was supported by grants from the US National Institutes of Health, AI046985 and AI087625 to K.K., GM073913 to V.V.V. and S10RR027308 for purchase of the IVIS imager.",

year = "2011",

month = aug,

doi = "10.1038/nbt.1918",

language = "English (US)",

volume = "29",

pages = "757--761",

journal = "Nature Biotechnology",

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AU - Piatkevich, Kiryl D.

AU - Ting, Li Min

AU - Zhang, Jinghang

AU - Kim, Kami

AU - Verkhusha, Vladislav V.

N1 - Funding Information: We thank E. Giraud (Institute for Research and Development, France) for the plasmid encoding bacteriophytochrome from R. palustris, A. Ulijasz and R. Vierstra (both from University of Wisconsin) for the plasmid encoding the heme-oxygenase from Synechocystis sp. PCC6803 and B. Glick (University of Chicago), D. Chudakov and K. Lukyanov (both from Institute of Bioorganic Chemistry, Russia) for the plasmids encoding GFP-like far-red fluorescent proteins. We are grateful to D. Entenberg for the help with two-photon excitation measurements, A. Muesch and D. Cohen for the assistance with virus purification and providing GFP-encoding adenoviruses and R. Zheng for the help with size-exclusion chromatography (all from Albert Einstein College of Medicine). This work was supported by grants from the US National Institutes of Health, AI046985 and AI087625 to K.K., GM073913 to V.V.V. and S10RR027308 for purchase of the IVIS imager.

PY - 2011/8

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N2 - Imaging biological processes in mammalian tissues will be facilitated by fluorescent probes with excitation and emission bands within the near-infrared optical window of high transparency. Here we report a phytochrome-based near-infrared fluorescent protein (iRFP) with excitation and emission maxima at 690 nm and 713 nm, respectively. iRFP does not require an exogenous supply of the chromophore biliverdin and has higher effective brightness, intracellular stability and photostability than earlier phytochrome-derived fluorescent probes. Compared with far-red GFP-like proteins, iRFP has a substantially higher signal-to-background ratio in a mouse model due to its infrared-shifted spectra.

AB - Imaging biological processes in mammalian tissues will be facilitated by fluorescent probes with excitation and emission bands within the near-infrared optical window of high transparency. Here we report a phytochrome-based near-infrared fluorescent protein (iRFP) with excitation and emission maxima at 690 nm and 713 nm, respectively. iRFP does not require an exogenous supply of the chromophore biliverdin and has higher effective brightness, intracellular stability and photostability than earlier phytochrome-derived fluorescent probes. Compared with far-red GFP-like proteins, iRFP has a substantially higher signal-to-background ratio in a mouse model due to its infrared-shifted spectra.

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Bright and stable near-infrared fluorescent protein for in vivo imaging

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