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. 2023 Feb 2;9:14. doi: 10.1038/s41531-023-00458-4

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© The Author(s) 2023

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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Fig. 1 — The glass surface of a microtiter plate is coated with a capture antibody (Syn211) against amino acid residues 121–125 of α-synuclein. The capture antibody binds both α-synuclein monomers and aggregates in the sample. The detection antibody (Syn211), a 1:1 mixture of this antibody labeled with fluorescent dye CF633 or CF488A, can only detect aggregates since it is directed against the same epitope as the capture antibody. The epitope on the monomer bound to the capture antibody is masked by the capture antibody and can, thus, not be bound by the detection antibody. The microtiter plate wells are imaged by two-channel confocal fluorescence microscopy to detect single particles. Only particles decorated with at least two different detection antibodies (colocalized signal) contribute to the sFIDA readout signal. The image was created with BioRender.com.