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. 2018 May 1;8:6795. doi: 10.1038/s41598-018-25009-3

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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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Chemical structures of peptoid-based mimics of SP-B (pB)²⁶ and SP-C (pC)²⁷. The eight N-terminal residues of pC contain side chains that are analogous to SP-C_5–12, and the remaining 14 aromatic hydrophobic residues form a helix that mimics the membrane spanning, hydrophobic helix of native SP-C. The N-terminal octadecyl amine of pC is a motif intended to mimic the post-translational modification of palmitoylated residues 5 and 6 in human SP-C. The mimic pB was designed to emulate the insertion region and helical amphipathic patterning of SP-B_1-25, with the added feature of an N-terminal octadecylamine.