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. 2022 Feb 7;11:7. doi: 10.1186/s40035-022-00283-4

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 5 — RT-QuIC reaction products seeded from MSA α-synuclein fibrils are conformationally distinguishable from RT-QuIC reaction products seeded from PD-derived fibrils. a, b Conformational stability assays for the RT-QuIC-derived MSA and PD fibrils. Representative α-synuclein immunoblots (a) and the resultant denaturation curves (b) are shown. MSA-derived fibrils are less stable than PD-derived fibrils in the epitope (amino acids 15–123) used to probe the structure. c Immunoblots of PBS-soluble α-synuclein species in brain homogenates from PD and MSA patients and their RT-QuIC-derived fibrils with thermolysin (TL) digestion. TL-resistant α-syn species were present in MSA and PD brain extracts, but TL-resistant α-syn species were only detectable in the MSA RT-QuIC-derived fibrils