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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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Amyloid formation by β-PV isoforms. (a) ThT-binding kinetics of gmPV1 (solid black symbols), gmPV2 (open black symbols), sjPV1 (solid orange symbols) and sjPV2 (open orange symbols) under acidic (square) and neutral (circle) aggregation conditions. (b) SDS-PAGE analysis of β-PV monomer conservation during amyloid formation at neutral pH. The full-length gel is displayed in supplementary Fig. 5S. (c) Intensity of ThT fluorescence as a function of the concentration of β-PV monomers. Values correspond to kinetics performed at pH 7.5 in the presence of EDTA. (d) Aggregation kinetics of 75 μM PV1 in the absence and presence of 15 μM PV2 (e) obtained experimentally in mixed reactions or (t) generated theoretically summing the traces of each of the chains.