LEPAE, Department of Chemical Engineering, Faculty of Engineering, University of Porto, Rua Roberto Frias, Porto, Portugal.
J Pept Sci. 2013 Sep;19(9):581-7. doi: 10.1002/psc.2535. Epub 2013 Aug 6.
The amyloid β-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 Aβ(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 Aβ(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 Aβ(₁₋₄₂) fibril formation.
β-淀粉样肽由 42 个氨基酸组成，是阿尔茨海默病斑块中细胞外淀粉样沉积物的主要成分。由于该过程速度很快，并且受到许多变量的影响，因此难以控制肽的自组装。在本文中，我们描述了不同带电和不带电表面活性剂对 Aβ（1-42）纤维形成的影响，以确定常见的替代聚集途径。通过超微结构分析、硫黄素 T 测定和二级结构分析对肽-表面活性剂相互作用进行了表征，结果表明带电表面活性剂通过静电相互作用与 Aβ（1-42）相互作用。带电胶束会减缓聚集过程并使肽稳定在寡聚状态，而不带电的表面活性剂则会促进 Aβ（1-42）纤维的形成。
