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

GS Filonov, KD Piatkevich, LM Ting, J Zhang… - Nature …, 2011 - nature.com
GS Filonov, KD Piatkevich, LM Ting, J Zhang, K Kim, VV Verkhusha
Nature biotechnology, 2011nature.com
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 …
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.
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