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Updated: Jun 11, 2025

Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease
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Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease

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揭示了CaCl2对粉样β聚合通过超临界角拉曼和光光谱和显微镜的作用

Nathalia Simea Münch1, Subir Das1, Stefan Seeger1

  • 1Department of Chemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland. sseeger@chem.uzh.ch.

Physical chemistry chemical physics : PCCP
|October 7, 2024
PubMed
概括

离子显著影响粉样β聚合,特别是粉样β 1-42 变体. 这项研究表明,离子保护脂质膜免受粉样β蛋白的插入,为阿尔茨海默病的机制提供了洞察力.

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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids08:53

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

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相关概念视频

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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