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Updated: Aug 16, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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表面诱导的α-Synuclein在不同大小的纳米颗粒上的形状变化,与蛋白质结构域相对应:来自增强采样MD模拟的洞察力

Shuai Gong1, Yu Ma1, Hongyi Liu1

  • 1Hubei Key Laboratory of Nanomedicine for Neurodegenerative Diseases, School of Chemistry, Chemical Engineering and Life Science, Institute WUT-AMU, Wuhan University of Technology, Wuhan 430070, China.

Langmuir : the ACS journal of surfaces and colloids
|April 15, 2025
PubMed
概括

中等尺寸的纳米粒子稳定了像α-synuclein (αS) 这样的内在无序的蛋白质. 较小或较大的纳米粒子促进容易聚合的结构,影响蛋白质构成和治疗应用.

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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...