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. 2019 Mar 12;9:4183. doi: 10.1038/s41598-019-40205-5

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© The Author(s) 2019

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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Nec-1 disaggregates synthetic Aβ aggregates. (A) Chemical structures of Nec-1 and demethylated Nec-1 (Nec-1i). (B) ThT assays for disaggregation of synthetic Aβ aggregates by two chemicals and only Nec-1 showed disaggregation effects. Fluorescence intensity was normalized to Aβ aggregates without compound treatments (100%). Cell viability assays using MTT in (C) HT22 neuronal cell line and (D) BV2 microglial cell line. Nec-1 or Nec-1i were treated to cells with pre-formed Aβ aggregates. Only Nec-1 inhibited Aβ-induced cell death. (E) Characterization and (F) quantification of Aβ42 peptides distribution by SDS-PAGE analysis with PICUP describing that Nec-1 reduced both oligomers and fibrils of to Aβ. All data presented are representative results of at least three independent experiments. Data is presented as mean ± SEM. *P ≤ 0.05, **P ≤ 0.01 and ***P ≤ 0.001 (One-way ANOVA followed by Bonferroni’s post-hoc comparison tests).