Engineering of bacterial phytochromes for near-infrared imaging, sensing, and light-control in mammals

Kiryl D. Piatkevich, Fedor V. Subach, Vladislav Verkhusha

Research output: Contribution to journalArticle

90 Citations (Scopus)

Abstract

Near-infrared light is favourable for imaging in mammalian tissues due to low absorbance of hemoglobin, melanin, and water. Therefore, fluorescent proteins, biosensors and optogenetic constructs for optimal imaging, optical readout and light manipulation in mammals should have fluorescence and action spectra within the near-infrared window. Interestingly, natural Bacterial Phytochrome Photoreceptors (BphPs) utilize the low molecular weight biliverdin, found in most mammalian tissues, as a photoreactive chromophore. Due to their near-infrared absorbance BphPs are preferred templates for designing optical molecular tools for applications in mammals. Moreover, BphPs spectrally complement existing genetically-encoded probes. Several BphPs were already developed into the near-infrared fluorescent variants. Based on the analysis of the photochemistry and structure of BphPs we suggest a variety of possible BphP-based fluorescent proteins, biosensors, and optogenetic tools. Putative design strategies and experimental considerations for such probes are discussed.

Original languageEnglish (US)
Pages (from-to)3441-3452
Number of pages12
JournalChemical Society Reviews
Volume42
Issue number8
DOIs
StatePublished - Apr 21 2013

Fingerprint

Phytochrome
Mammals
Infrared imaging
Infrared radiation
Biosensors
Biliverdine
Tissue
Imaging techniques
Photochemical reactions
Melanins
Chromophores
Hemoglobins
Proteins
Fluorescence
Molecular weight
Water

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Engineering of bacterial phytochromes for near-infrared imaging, sensing, and light-control in mammals. / Piatkevich, Kiryl D.; Subach, Fedor V.; Verkhusha, Vladislav.

In: Chemical Society Reviews, Vol. 42, No. 8, 21.04.2013, p. 3441-3452.

Research output: Contribution to journalArticle

@article{b4ef2df837e244f48f5c80f7b6ce9da6,
title = "Engineering of bacterial phytochromes for near-infrared imaging, sensing, and light-control in mammals",
abstract = "Near-infrared light is favourable for imaging in mammalian tissues due to low absorbance of hemoglobin, melanin, and water. Therefore, fluorescent proteins, biosensors and optogenetic constructs for optimal imaging, optical readout and light manipulation in mammals should have fluorescence and action spectra within the near-infrared window. Interestingly, natural Bacterial Phytochrome Photoreceptors (BphPs) utilize the low molecular weight biliverdin, found in most mammalian tissues, as a photoreactive chromophore. Due to their near-infrared absorbance BphPs are preferred templates for designing optical molecular tools for applications in mammals. Moreover, BphPs spectrally complement existing genetically-encoded probes. Several BphPs were already developed into the near-infrared fluorescent variants. Based on the analysis of the photochemistry and structure of BphPs we suggest a variety of possible BphP-based fluorescent proteins, biosensors, and optogenetic tools. Putative design strategies and experimental considerations for such probes are discussed.",
author = "Piatkevich, {Kiryl D.} and Subach, {Fedor V.} and Vladislav Verkhusha",
year = "2013",
month = "4",
day = "21",
doi = "10.1039/c3cs35458j",
language = "English (US)",
volume = "42",
pages = "3441--3452",
journal = "Chemical Society Reviews",
issn = "0306-0012",
publisher = "Royal Society of Chemistry",
number = "8",

}

TY - JOUR

T1 - Engineering of bacterial phytochromes for near-infrared imaging, sensing, and light-control in mammals

AU - Piatkevich, Kiryl D.

AU - Subach, Fedor V.

AU - Verkhusha, Vladislav

PY - 2013/4/21

Y1 - 2013/4/21

N2 - Near-infrared light is favourable for imaging in mammalian tissues due to low absorbance of hemoglobin, melanin, and water. Therefore, fluorescent proteins, biosensors and optogenetic constructs for optimal imaging, optical readout and light manipulation in mammals should have fluorescence and action spectra within the near-infrared window. Interestingly, natural Bacterial Phytochrome Photoreceptors (BphPs) utilize the low molecular weight biliverdin, found in most mammalian tissues, as a photoreactive chromophore. Due to their near-infrared absorbance BphPs are preferred templates for designing optical molecular tools for applications in mammals. Moreover, BphPs spectrally complement existing genetically-encoded probes. Several BphPs were already developed into the near-infrared fluorescent variants. Based on the analysis of the photochemistry and structure of BphPs we suggest a variety of possible BphP-based fluorescent proteins, biosensors, and optogenetic tools. Putative design strategies and experimental considerations for such probes are discussed.

AB - Near-infrared light is favourable for imaging in mammalian tissues due to low absorbance of hemoglobin, melanin, and water. Therefore, fluorescent proteins, biosensors and optogenetic constructs for optimal imaging, optical readout and light manipulation in mammals should have fluorescence and action spectra within the near-infrared window. Interestingly, natural Bacterial Phytochrome Photoreceptors (BphPs) utilize the low molecular weight biliverdin, found in most mammalian tissues, as a photoreactive chromophore. Due to their near-infrared absorbance BphPs are preferred templates for designing optical molecular tools for applications in mammals. Moreover, BphPs spectrally complement existing genetically-encoded probes. Several BphPs were already developed into the near-infrared fluorescent variants. Based on the analysis of the photochemistry and structure of BphPs we suggest a variety of possible BphP-based fluorescent proteins, biosensors, and optogenetic tools. Putative design strategies and experimental considerations for such probes are discussed.

UR - http://www.scopus.com/inward/record.url?scp=84878742725&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84878742725&partnerID=8YFLogxK

U2 - 10.1039/c3cs35458j

DO - 10.1039/c3cs35458j

M3 - Article

C2 - 23361376

AN - SCOPUS:84878742725

VL - 42

SP - 3441

EP - 3452

JO - Chemical Society Reviews

JF - Chemical Society Reviews

SN - 0306-0012

IS - 8

ER -