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. 2019 Feb 25;9:2689. doi: 10.1038/s41598-019-38749-7

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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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Model for the membrane pore formed by the Aβ_25–35 peptide, as viewed along the pore central axis (top view). The pore complex is a hexamer of 6-stranded β-barrel-like structures. The barrel structure is constructed based on the backbone structure of αB crystallin residues 90–100 (PDB entry 3sgn)⁸⁶, side chains replaced with those of Aβ_25–35. Each barrel is turned about its cylindrical axes by 60 degrees relative to its neighbors. The diameter of the central ion-conducting cavity is around 13Å, as shown.