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-β peptide (Aβ) under near-infrared (NIR) light irradiation. On the basis of the structure of a fluorescent Aβ 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 Aβ by 9 under NIR irradiation in the presence of cells attenuated the cytotoxicity of Aβ. The tissue permeability of NIR enabled catalytic photooxygenation of aggregated Aβ 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 Aβ level in the brain.

淀粉样肽和蛋白质的有毒聚集与许多人类疾病（包括阿尔茨海默氏病（AD））密切相关。在这里，我们开发了生物相容性光氧合催化剂9，它可以在近红外（NIR）光照射下选择性地氧化和降解AD相关淀粉样β肽（Aβ）的致病性聚集。根据荧光Aβ探针CRANAD-2的结构，引入了溴原子以增加用于光氧合的单线态氧的产生。分别使用菊糖苷和全氟烷基硼酸酯部分作为电子给体和-受体组分，显着增强了光催化活性并降低了光毒性。聚集的Aβ被9光氧化NIR照射下在细胞存在下减弱了Aβ的细胞毒性。NIR的组织渗透性使小鼠皮肤下聚集的Aβ能够进行催化光氧化。此外，将催化剂与近红外光照射一起注射到AD模型小鼠的大脑中会导致大脑中完整Aβ水平的显着降低。