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. 2018 Jul 9;8:10353. doi: 10.1038/s41598-018-28649-7

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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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Typical β-barrel oligomers formed by hIAPP22–28, Aβ16–22 and NACore shown with both top and side views. The peptides were shown in cartoon representation with side-chains shown as sticks and colored according to residue types (hydrophobic in white, hydrophilic in green, positively charged in blue, and negatively charged in red). The sequence of each amyloid fragment was also given at the bottom.