Capillary electrophoresis studies on the aggregation process of β‐amyloid 1‐42 and 1‐40 peptides
Capillary electrophoresis studies on the aggregation process of β‐amyloid 1‐42 and 1‐40 peptides
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DOI：
10.1002/elps.200406062
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发表时间：
2004-10
期刊：
影响因子：
2.9
通讯作者：
S. Sabella;M. Quaglia;C. Lanni;M. Racchi;S. Govoni;G. Caccialanza;A. Calligaro;V. Bellotti;E. De Lorenzi
中科院分区：
文献类型：
--
作者：
S. Sabella;M. Quaglia;C. Lanni;M. Racchi;S. Govoni;G. Caccialanza;A. Calligaro;V. Bellotti;E. De Lorenzi
描述了在溶液中监测β-淀粉样蛋白（Aβ）成核步骤的可能性，从而通过使用毛细管电泳和优化的实验条件来描述该动态过程。本文显示了Aβ 1 - 42和Aβ 1 - 40随时间推移的电泳图谱的显著差异，并阐明了不同的聚集状态，这反映了两种非常相似的肽的非常不同的寡聚化行为。通过超离心分离一种聚集的高分子量物质，使我们能够评估其作为有毒低聚物的作用。通过添加小分子对鉴定的物质之间的现有平衡的扰动原则上可以干扰肽的聚集过程并最终防止体外噬斑形成。
The possibility to monitor, in solution, the steps of β‐amyloid (Aβ) nucleation and therefore to describe this dynamic process by using capillary electrophoresis and under optimized experimental conditions is described. Striking differences in the electrophoretic patterns of Aβ 1‐42 and Aβ 1‐40 over time are here shown, and different aggregation states are elucidated, which reflect the very diverse oligomerization behavior of two very similar peptides. The isolation of one aggregated species of high molecular weight by ultracentrifugation allowed us to assess its role as toxic oligomer. The perturbation of the existing equilibrium among the identified species by the addition of small molecules can in principle interfere with the aggregation process of the peptides and ultimately prevent the plaque formation in vitro.