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. 2019 Aug 8;8:24. doi: 10.1186/s40035-019-0164-x

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© The Author(s). 2019

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 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.

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Fig. 1 — RT-QuIC analysis of in vitro generated α-synuclein aggregates. a In vitro generation of α-synuclein aggregates (artificial seeds). rec-αS [140 μM] was induced to aggregate by alternating cycles of incubation and shaking. Average ThT fluorescence intensity was plotted against time; b TEM analysis of final α-synuclein aggregates. Amyloid fibrils were efficiently generated in vitro under well controlled experimental conditions. Scale bar: 500 nm; c Assessment of the RT-QuIC detection limits. Serial dilutions of the artificial seeds previously produced were analyzed by means of RT-QuIC. All dilutions efficiently accelerated the kinetics of rec-αS aggregation. Average ThT fluorescence intensity was plotted against time. Self-assembly refers to unseeded rec-αS reactions