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Updated: Jun 13, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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直接观察粉样蛋白自我组装中的核和生长

Yan Liang1, David G Lynn, Keith M Berland

  • 1The Center for Fundamental and Applied Molecular Evolution and the Center for Chemical Evolution, Department of Chemistry, Emory University, 1515 Dickey Drive, Atlanta, Georgia 30322, USA.

Journal of the American Chemical Society
|April 20, 2010
PubMed
概括

研究人员观察了阿尔茨海默氏症早期的阿贝塔组合,揭示了核化粉样蛋白生长的动态聚合物. 这一发现通过直接观察粉样蛋白组合来统一蛋白质错折疾病模型.

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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, normally used to...
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, normally used to...