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. 2024 May 13;14:10868. doi: 10.1038/s41598-024-61691-2

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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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Representative MALDI mass spectra for water-extracted CAA fibrils from leptomeningeal tissues of the indicated AD subjects. Prior to MALDI, CAA fibrils were immunoprecipitated with Dynabeads M-280 sheep anti-mouse beads coupled to 6E10 or 4G8 antibodies. (a) Mass spectra for the indicated study subjects, showing Aβ-assigned peaks that were analyzed using an in-house script that matched the masses of the observed peaks to those of known Aβ peptides. (b) The relative abundance of Aβ peptides identified in each sample.