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. 2020 Mar 20;10:5138. doi: 10.1038/s41598-020-62115-7

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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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Amyloidophilic dye uptake assays. Ten micrograms of purified recombinant C123 (red bars), AgA (blue bars), or Smu_63c (green bars) were reacted with ThT, CDy11, BD-oligo, and MK-H4. Empty bars correspond to the purified monomeric proteins, solid bars to the samples after amyloid induction, and diagonal patterned bars to the purified amyloid fibers after treatment of the amyloid material to remove residual monomers. C123 and AgA polypeptides correspond to naturally occurring amyloidogenic derivatives of P1 and WapA, respectively. Arbitrary units (a.u.) ThT (Excitation = 440, Emission = 485), CDy11 and BD-Oligo (Ex = 530, Em = 580), and MK-H4 (Ex = 475, Em = 567). Protein concentration 0.1 mg/mL. Error bars represent standard deviations.