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. 2018 Nov 20;8:17127. doi: 10.1038/s41598-018-35431-2

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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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Depiction of how the hydrophobic amino acid backbones may self-assemble in an anti-parallel manner to accommodate the different sizes of the amino acid side chains. The darker the tone, the larger the side chain. Indigo refers to the hydrophobic amino acid and yellow refers to the hydrophilic C-terminal amino acid (Xaa). For X = (A–C) the peptides are amidated at the C-terminal (viz. a carboxamide); for X = (D, E) the C-terminal is a carboxylic acid.