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Updated: Sep 15, 2025

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氨基酸β调节α-synuclein的相分离和聚合

Alexander Röntgen1, Zenon Toprakcioglu1, Owen M Morris1

  • 1Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America
|July 14, 2025
PubMed
概括

粉样β (Aβ) 变体在神经退行性疾病中对α-synuclein (αSyn) 聚合有不同的影响. Aβ42启动αSyn相分离,而Aβ40加速其粉样蛋白形成.

关键词:
化学动力学 化学动力学液态-液态相隔离方法 液态相隔离方法蛋白质聚合蛋白质的聚合物蛋白质凝结凝结的过程

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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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