化学和机制分析光动力抑制阿尔茨海默病β-淀粉样蛋白聚集。
Chemical and mechanistic analysis of photodynamic inhibition of Alzheimer's β-amyloid aggregation.
机构信息
Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
KAIST Institute for the BioCentury, Department of Materials Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Republic of Korea.
出版信息
Chem Commun (Camb). 2019 Jan 25;55(8):1152-1155. doi: 10.1039/c8cc09288e. Epub 2019 Jan 11.
The self-assembly of the beta-amyloid peptide (Aβ) into amyloid aggregates is a central phenomenon associated with Alzheimer's disease. Here, we report chemical modifications of key amino acid residues of Aβ (Y10, H13, H14, and M35) by photoexcited thioflavin-T (ThT), a fluorescent probe of amyloid structure. The quantitative chemical kinetics analysis shows that the oxidized monomer species does not self-assemble, nor perturb the aggregation kinetics of non-oxidized Aβ.
β-淀粉样肽（Aβ）自组装成淀粉样聚集体是与阿尔茨海默病相关的中心现象。在这里，我们报告了通过光激发的硫黄素 T（ThT）对 Aβ（Y10、H13、H14 和 M35）的关键氨基酸残基进行化学修饰，ThT 是淀粉样结构的荧光探针。定量化学动力学分析表明，氧化单体物种不会自组装，也不会干扰未氧化 Aβ的聚集动力学。
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