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. 2017 Aug 25;7:9520. doi: 10.1038/s41598-017-10422-x

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© The Author(s) 2017

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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Isolation and comparison of Aβ proteoforms from human AD brain. Workflow for isolation of endogenous Aβ proteoforms. Cortical tissue was dounce homogenized with sub-critical micelle concentration of CHAPS followed by differential ultracentrifugation, anti-Aβ dual antibody immunoprecipitation, and elution in neat formic acid. Immunoprecipitated Aβ proteoforms in the HMW soluble aggregates fractions and more insoluble fractions were precipitated and purified from undigested non-Aβ proteins using C₈ TopTips and analyzed by nLC-MS/MS. RCF, relative centrifugal force; Sol., soluble; LMW, low molecular weight; HMW, high molecular weight; IP, immunoprecipitation; pptn., precipitation; SPE, solid phase extraction.