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. 2020 Jan 14;10:235. doi: 10.1038/s41598-019-57143-x

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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(A,B) Aggregation kinetics of Aβ₄₂ at different concentrations from 1.0 (violet) to 9.0 μM (red) recorded by ThT fluorescence experiments fitted with a multi-step (A) and simple secondary nucleation model (B). The kinetic traces fit best to the multi-step secondary nucleation model, reflected by a lower χ² value. (C) Aggregation half times, 𝜏_1/2, plotted against the initial peptide concentration, [Aβ], exhibit a γ coefficient of γ = −1.0 ± 0.1. (D) The final ThT intensity of the normalized aggregation traces in (A) exhibits a linear relation to [Aβ].