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. 2019 Nov 8;9:16298. doi: 10.1038/s41598-019-52801-6

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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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Features of the amyloid aggregates formed by β-PV isoforms. (a) Far-UV CD spectra of the insoluble aggregates of gmPV1, gmPV2 and sjPV2. (b) Dot blot analysis of (A) β-PV aggregates using amyloid-specific anti-fibril (OC) and anti-oligomer (A11) antibodies. (G) Ca²⁺-bound chains were included as controls. (c) Coomassie blue-stained SDS-PAGE gel of the harsh proteinase K and pepsin digestions of gmPV1, gmPV2 and sjPV2 amyloid aggregates. The original membranes and gels of panels b and c are displayed in supplementary Fig. 6S.