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. 2018 Mar 19;8:4772. doi: 10.1038/s41598-018-23122-x

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© The Author(s) 2018

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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ZnAβ40 oligomer can be restored rapidly back to fibrillization pathway by EDTA. (A,E) Aβ and ZnAβ40 (A) or ZnAβ42 (E) aggregation monitored by ThT assay. Three folds of EDTA was added when Aβ fibrillization reached a plateau. The time of addition is indicated by arrows. (B,F) Time-course conformation changes of ZnAβ40 or ZnAβ42 after EDTA treatment measured by far-UV CD. (C,D and G,H) TEM images (C and G) and dot blotting (D,H) of the time course samples in the aggregation. Scale bars in TEM images are 100 nm. ZnAβ was first prepared and incubated for 1 day for ZnAβ oligomer formation prior to EDTA treatment in the CD and dot blotting experiments. Dot blotted membrane was probed with A11 and OC antibody and stained by Direct blue as a dotting control.