Scholarlink

<p>Deposition of amyloid proteins and their associated interactome is a hallmark of Alzheimer’s disease (AD) and other amyloidosis diseases, with their composition implying disease etiology. However, precise in-situ micro-dissection of amyloid deposits in AD brain tissue remains a challenge. In this work, we first divert the excited state energy of Thioflavin T from singlet fluorescence to triplet photocatalytic amyloid protein labeling through molecular engineering, while maintain its pan-amyloid binding affinity and selectivity. We further demonstrate that the amyloid labeling is catalyzed via type-I radical-based photosensitization with diverse residue modification sites. In female AD mouse brain tissue without homogenization, Amyloid-ID in-situ captures and profiles amyloid deposits, reliably reporting the often-lost tau biomarker. Finally, we provide comparative amyloidomics resources across 3 commonly used AD mouse models, revealing conjunct mitochondrial entangling pattern within amyloid deposits. Overall, we report a photocatalytic proteomics strategy (namely Amyloid-ID) to profile amyloid deposits directly from AD brain tissue.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Amyloid-ID: photocatalytic profiling of amyloid deposits in Alzheimer’s disease tissue

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年1月9日

查看全文
  • Huan Feng,
  • Qun Zhao,
  • Fangliang Guo,
  • Jing Yan,
  • Nan Zhao,
  • Junbao Ma,
  • Rui Sun,
  • Kaini Shen,
  • Yusong Ge,
  • Xin Zhang,
  • Lihua Zhang,
  • Yu Liu

摘要

Deposition of amyloid proteins and their associated interactome is a hallmark of Alzheimer’s disease (AD) and other amyloidosis diseases, with their composition implying disease etiology. However, precise in-situ micro-dissection of amyloid deposits in AD brain tissue remains a challenge. In this work, we first divert the excited state energy of Thioflavin T from singlet fluorescence to triplet photocatalytic amyloid protein labeling through molecular engineering, while maintain its pan-amyloid binding affinity and selectivity. We further demonstrate that the amyloid labeling is catalyzed via type-I radical-based photosensitization with diverse residue modification sites. In female AD mouse brain tissue without homogenization, Amyloid-ID in-situ captures and profiles amyloid deposits, reliably reporting the often-lost tau biomarker. Finally, we provide comparative amyloidomics resources across 3 commonly used AD mouse models, revealing conjunct mitochondrial entangling pattern within amyloid deposits. Overall, we report a photocatalytic proteomics strategy (namely Amyloid-ID) to profile amyloid deposits directly from AD brain tissue.