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. 2019 Jun 13;9:8622. doi: 10.1038/s41598-019-45075-5

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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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BP100 initial structures: random coil L-BP100 (a) and alpha-helical α-BP100 (b). Helical wheel projection (c), Lys5 and Ile7 were used as representative residues of polar and apolar moieties, respectively. In (d) DPPC (in blue) and DPPG (in yellow). Atom names are shown for peptide and lipids; they were used in our peptide-lipid pair analysis.