Journal
CHEM
Volume 4, Issue 4, Pages 807-820Publisher
CELL PRESS
DOI: 10.1016/j.chempr.2018.02.008
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Funding
- Japan Science and Technology Agency ERATO grant [JPMJER1103]
- Japan Society for the Promotion of Science [16H06216, 15H02492, 17K19480]
- Grants-in-Aid for Scientific Research [17K19480, 15H02492, 17H06442, 17K19479, 17K13260] Funding Source: KAKEN
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Toxic aggregation of amyloid peptide and protein is intimately related to a number of human diseases, including Alzheimer's disease (AD). Here, we developed biocompatible photooxygenation catalyst 9, which can selectively oxygenate and degrade the pathogenic aggregation of AD-related amyloid-beta peptide (A beta) under near-infrared (NIR) light irradiation. On the basis of the structure of a fluorescent A beta probe, CRANAD-2, a bromine atom was introduced to increase the production of singlet oxygen for photooxygenation. The use of julolidine and perfluoroalkylborate moieties as electron-donor and -acceptor components, respectively, markedly enhanced the photocatalytic activity and reduced phototoxicity. Photooxygenation of aggregated A beta by 9 under NIR irradiation in the presence of cells attenuated the cytotoxicity of A beta. The tissue permeability of NIR enabled catalytic photooxygenation of aggregated A beta under the mouse skin. Moreover, injection of the catalyst to the AD-model mouse brain along with NIR light irradiation led to a significant decrease in the intact A beta level in the brain.
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