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. 2018 Jan 16;9:234. doi: 10.1038/s41467-017-02742-3

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© The Author(s) 2018

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. 5 — Regio-specific and stereo-specific addition reactions with the (OV)₄/V(DV)₄ amyloid. Reverse-phase HPLC chromatograms of the addition reactions with valine (a), phenylalanine (b), DL-valine (c) and DL- phenylalanine (d). Reactions with just substrate (OV)₄ are the black traces and those with the amyloid (OV)₄/V(DV)₄ are the red ones. The ornithine sidechain addition products are indicated with the superscript S.C. The * indicates the C-terminal deamidated substrate that remained after purification. The (OV)₄ concentration was 100 μM, the V(DV)₄ concentration was 120 μM and amino acids were all at 200 μM of each enantiomer. The addition product to the N-terminus was identified via NMR and reverse-phase HPLC analysis of an authentic V(OV)₄ control peptide (see Supplementary Fig. 10)