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. 2019 Feb 28;9:3123. doi: 10.1038/s41598-019-39781-3

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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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X-ray fibre diffraction (XRFD) patterns from partially aligned fibrils formed by synthetic peptides (A) Ser30b-Trp35 and (B) Ile30-Gln37 incubated in MilliQ-quality water plus Na azide 0.05%, as described in Methods. (D,E) show transmission electron micrographs of the aggregates whose XRFD pattern are shown in panels A and B, respectively. The images were obtained with a HITACHI-7100 transmission electron microscope (C). Comparison of the experimental XRFD pattern of the aggregates of the peptide Ser30b-Trp35, as shown in (A), and the simulated pattern (inserted quadrant) calculated based on the theoretical model shown in (F). Black arrows are shown to highlight positions of matching major diffraction signal positions on the equator and meridian. (F) Structural model of the steric zipper of peptide Ser30b-Trp35, generated by the computational tool ZipperDB²⁶. The amino acid side chains are shown in stick representation and named with the one-letter code. The dotted lines represent intra- and interpeptide H-bonds stabilizing the crystal lattice. Figure prepared with PyMOL⁷⁰.