Charged surfactants induce a non-fibrillar aggregation pathway of amyloid-beta peptide
Charged surfactants induce a non-fibrillar aggregation pathway of amyloid-beta peptide
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DOI：
10.1002/psc.2535
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发表时间：
2013-09-01
影响因子：
2.1
通讯作者：
Pereira, Maria do Carmo
中科院分区：
文献类型：
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作者：
Loureiro, Joana A.;Rocha, Sandra;Pereira, Maria do Carmo
具有42个氨基酸序列的淀粉样蛋白肽是阿尔茨海默病斑块中细胞外淀粉样蛋白沉积的主要成分。由于多肽自组装过程快速且受许多变量的影响，因此难以实现对其的控制。在本文中，我们描述了不同的带电和非带电表面活性剂对A（(1-42)）纤颤的影响，以定义常见的交替聚集途径。通过超结构分析、硫黄素T测定和二级结构分析对肽-表面活性剂相互作用的表征表明，带电荷的表面活性剂通过静电相互作用与A（(1-42)）相互作用。带电荷的胶束减缓了聚集过程，使肽稳定在寡聚态，而不带电荷的表面活性剂促进了A（(1-42)）纤维的形成。版权所有(c) 2013欧洲多肽协会和约翰威利父子有限公司
The amyloid -peptide with a sequence of 42 amino acids is the major constituent of extracellular amyloid deposits in Alzheimer's disease plaques. The control of the peptide self-assembly is difficult to achieve because the process is fast and is affected by many variables. In this paper, we describe the effect of different charged and non-charged surfactants on A((1-42)) fibrillation to define common alternate aggregation pathways. The characterization of the peptide-surfactant interactions by ultra-structural analysis, thioflavin T assay and secondary structure analysis, suggested that charged surfactants interact with A((1-42)) through electrostatic interactions. Charged micelles slow down the aggregation process and stabilize the peptide in the oligomeric state, whereas non-charged surfactants promote the A((1-42)) fibril formation. Copyright (c) 2013 European Peptide Society and John Wiley & Sons, Ltd.