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. 2019 Apr 2;9:5522. doi: 10.1038/s41598-019-41897-5

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© The Author(s) 2019

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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Structure of Aβ1-15 glycopeptide standard 1 and schematic protocol for the Aβ immunopurification and LC-MS/MS of CSF samples. (A) Structure of Galβ3GalNAcα1-O-Tyr glycosylated Aβ1-15 having ¹⁵N and ¹³C isotope labels on Asp-1 and ¹³C on the GalNAc N-acetyl group. (B) The 1 and Aβ1-15** internal standards were added to CSF samples and co-immunopurified using antibody 6E10 coated magnetic beads. The co-immunopurified internal standards as well as native Aβ peptides and glycopeptides, from QC samples, were directly subjected to LC-MS/MS (Route 1) or to acid hydrolysis of sialic acid residues, QC and patient samples, and then analyzed with the PRM assay (Route 2). A range of Aβ peptides and glycopeptides were co-immunopurified, but only Aβ1-15, glycosylated Aβ1-15, Aβ1-17, and glycosylated Aβ1-17 were included in the PRM assay.