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. 2024 Mar 27;15:2677. doi: 10.1038/s41467-024-46898-1

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© The Author(s) 2024

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 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/.

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Fig. 1 — a Workflow of the semi-synthesis of α-syn with different modifications at S87. b Left: ThT kinetic assay (top) and NS-TEM images (bottom) of unmodified WT, gS87, and pS87 α-syn fibrils. Right: ThT kinetic assay (top) and NS-TEM images (bottom) of unmodified WT, gS87 and pS87 α-syn fibrils in the presence of 1 mol% PFF formed by the unmodified WT α-syn monomer. Zoom-in views of gS87 and pS87 ThT kinetic assay were shown. The fibrils were characterized by NS-TEM at the endpoint (60 h) of the ThT kinetic assay. Data correspond to mean ± s.d., n = 3 (replicates). Scale bar: 200 nm. c AFM images of gS87 α-syn, pS87 α-syn, and unmodified WT α-syn fibril. The arrows at both sides of the fibril indicate the starting points of the fibril protrusions to clarify the handedness. Fibrils formed by gS87, pS87 and WT in >3 independent experiments provide reproducible images and their data were analyzed in Nanoscope software. Scale bar: 200 nm. Source data are provided as a Source Data file.