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. 2021 Dec 6;11:23440. doi: 10.1038/s41598-021-02898-5

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© The Author(s) 2021

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Hexapeptides derived from P10 and P4 (only a single stretch) form steric zippers in silico. P10 (a) and P4 (b) sequences were analyzed by Cordax (LOURO et al., 2020). The algorithm identified five hexapeptides in the sequence of P10 (TLIAIH, LIAIHT, IAIHTL, TLAIRY and HTLAIR) capable of forming steric zippers. Except for HTLAIR, each peptide forms two sheets (orange and red) composed of parallel β-strands (antiparallel in HTLAIR). In panel (a), the lower images show details of the interdigitation of the lateral chains of the amino acids in the steric zippers facing the interior of the bilayer. (b) Only one hexapeptide of P4 (TFITED; blue and green) adopts a steric zipper structure in an antiparallel fashion.