Open Access
Proceedings of the National Academy of Sciences of the United States of America, volume 105, issue 1, pages 28-32
Selective photoinactivation of protein function through environment-sensitive switching of singlet oxygen generation by photosensitizer
Yogo Takatoshi
1, 2
,
Urano Yasuteru
1, 3
,
MIZUSHIMA Akiko
4
,
Sunahara Hisato
1, 2
,
Inoue Takanari
1
,
Hirose Kenzo
5
,
IINO Masamitsu
4
,
Kikuchi Kazuya
6
,
Nagano Tetsuo
1, 2
1
*Graduate School of Pharmaceutical Sciences and
2
Core Research for Evolutional Science and Technology (CREST) and
3
Precursory Research for Embryonic Science and Technology (PRESTO), Japan Science and Technology Agency, 4-1-8 Honcho Kawaguchi, Saitama 332-0012, Japan;
|
4
Department of Pharmacology, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan;
|
5
Department of Cell Physiology, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa, Nagoya, Aichi 466-8550, Japan; and
|
6
Graduate School of Engineering, Division of Advanced Science and Biotechnology, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan
|
Publication type: Journal Article
Publication date: 2008-01-08
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 11.1
ISSN: 00278424, 10916490
PubMed ID:
18172220
Multidisciplinary
Abstract
Chromophore-assisted light inactivation is a promising technique to inactivate selected proteins with high spatial and temporal resolution in living cells, but its use has been limited because of the lack of a methodology to prevent nonspecific photodamage in the cell owing to reactive oxygen species generated by the photosensitizer. Here we present a design strategy for photosensitizers with an environment-sensitive off/on switch for singlet oxygen (1O2) generation, which is switched on by binding to the target, to improve the specificity of protein photoinactivation. 1O2 generation in the unbound state is quenched by photoinduced electron transfer, whereas 1O2 generation can occur in the hydrophobic environment provided by the target protein, after specific binding. Inositol 1,4,5-trisphosphate receptor, which has been suggested to have a hydrophobic pocket around the ligand binding site, was specifically inactivated by an environment-sensitive photosensitizer-conjugated inositol 1,4,5-trisphosphate receptor ligand without 1O2 generation in the cytosol of the target cells, despite light illumination, demonstrating the potential of environment-sensitive photosensitizers to allow high-resolution control of generation of reactive oxygen species in the cell.
Citations by journals
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1
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3
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5
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7
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Chemistry - A European Journal
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Chemical Reviews
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Russian Journal of General Chemistry
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Journal of Chemical Physics
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2 publications, 2.2%
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Tetrahedron
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2 publications, 2.2%
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Coordination Chemistry Reviews
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2 publications, 2.2%
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Angewandte Chemie
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Angewandte Chemie
2 publications, 2.2%
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Angewandte Chemie - International Edition
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Angewandte Chemie - International Edition
2 publications, 2.2%
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Advanced Functional Materials
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2 publications, 2.2%
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Macromolecules
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2 publications, 2.2%
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Organic Letters
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Organic Letters
2 publications, 2.2%
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ACS applied materials & interfaces
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2 publications, 2.2%
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RSC Advances
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RSC Advances
2 publications, 2.2%
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Chemical Communications
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Chemical Communications
2 publications, 2.2%
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Inorganica Chimica Acta
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Inorganica Chimica Acta
1 publication, 1.1%
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Inorganic Chemistry Communication
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Inorganic Chemistry Communication
1 publication, 1.1%
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Journal of Molecular Liquids
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Journal of Molecular Liquids
1 publication, 1.1%
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Assay and Drug Development Technologies
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Assay and Drug Development Technologies
1 publication, 1.1%
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Journal of Porphyrins and Phthalocyanines
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Journal of Porphyrins and Phthalocyanines
1 publication, 1.1%
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Pharmaceutics
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Pharmaceutics
1 publication, 1.1%
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Molecules
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Molecules
1 publication, 1.1%
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Biomolecules
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Biomolecules
1 publication, 1.1%
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Nature Communications
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Nature Communications
1 publication, 1.1%
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Scientific Reports
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Scientific Reports
1 publication, 1.1%
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Photochemical and Photobiological Sciences
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Photochemical and Photobiological Sciences
1 publication, 1.1%
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Biosensors and Bioelectronics
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1 publication, 1.1%
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1
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3
4
5
6
7
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Citations by publishers
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5
10
15
20
25
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American Chemical Society (ACS)
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American Chemical Society (ACS)
23 publications, 25.27%
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Elsevier
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Elsevier
20 publications, 21.98%
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Wiley
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Wiley
20 publications, 21.98%
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Royal Society of Chemistry (RSC)
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Royal Society of Chemistry (RSC)
11 publications, 12.09%
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Springer Nature
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Springer Nature
4 publications, 4.4%
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Pleiades Publishing
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Pleiades Publishing
3 publications, 3.3%
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Multidisciplinary Digital Publishing Institute (MDPI)
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Multidisciplinary Digital Publishing Institute (MDPI)
3 publications, 3.3%
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American Institute of Physics (AIP)
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American Institute of Physics (AIP)
2 publications, 2.2%
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Mary Ann Liebert
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Mary Ann Liebert
1 publication, 1.1%
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World Scientific
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World Scientific
1 publication, 1.1%
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Proceedings of the National Academy of Sciences (PNAS)
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Proceedings of the National Academy of Sciences (PNAS)
1 publication, 1.1%
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5
10
15
20
25
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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GOST
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Yogo T. et al. Selective photoinactivation of protein function through environment-sensitive switching of singlet oxygen generation by photosensitizer // Proceedings of the National Academy of Sciences of the United States of America. 2008. Vol. 105. No. 1. pp. 28-32.
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Yogo T., Urano Y., MIZUSHIMA A., Sunahara H., Inoue T., Hirose K., IINO M., Kikuchi K., Nagano T. Selective photoinactivation of protein function through environment-sensitive switching of singlet oxygen generation by photosensitizer // Proceedings of the National Academy of Sciences of the United States of America. 2008. Vol. 105. No. 1. pp. 28-32.
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RIS
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TY - JOUR
DO - 10.1073/pnas.0611717105
UR - https://doi.org/10.1073%2Fpnas.0611717105
TI - Selective photoinactivation of protein function through environment-sensitive switching of singlet oxygen generation by photosensitizer
T2 - Proceedings of the National Academy of Sciences of the United States of America
AU - Yogo, Takatoshi
AU - Urano, Yasuteru
AU - MIZUSHIMA, Akiko
AU - Sunahara, Hisato
AU - Inoue, Takanari
AU - Hirose, Kenzo
AU - IINO, Masamitsu
AU - Kikuchi, Kazuya
AU - Nagano, Tetsuo
PY - 2008
DA - 2008/01/08 00:00:00
PB - Proceedings of the National Academy of Sciences (PNAS)
SP - 28-32
IS - 1
VL - 105
PMID - 18172220
SN - 0027-8424
SN - 1091-6490
ER -
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@article{2008_Yogo,
author = {Takatoshi Yogo and Yasuteru Urano and Akiko MIZUSHIMA and Hisato Sunahara and Takanari Inoue and Kenzo Hirose and Masamitsu IINO and Kazuya Kikuchi and Tetsuo Nagano},
title = {Selective photoinactivation of protein function through environment-sensitive switching of singlet oxygen generation by photosensitizer},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
year = {2008},
volume = {105},
publisher = {Proceedings of the National Academy of Sciences (PNAS)},
month = {jan},
url = {https://doi.org/10.1073%2Fpnas.0611717105},
number = {1},
pages = {28--32},
doi = {10.1073/pnas.0611717105}
}
Cite this
MLA
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Yogo, Takatoshi, et al. “Selective photoinactivation of protein function through environment-sensitive switching of singlet oxygen generation by photosensitizer.” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 1, Jan. 2008, pp. 28-32. https://doi.org/10.1073%2Fpnas.0611717105.