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. 2021 Jun 18;6:85. doi: 10.1038/s41541-021-00347-y

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© The Author(s) 2021, corrected publication 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 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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Fig. 1 — a, i The sequences of peptides FsIIm, V-306p (Nle = l-norleucine, Dab = l-diaminobutyric acid, d-Ala = d-alanine), ii the synthetic lipopeptide (shown in single amino acid letter code, with the coiled-coil heptad repeat (IEKKIES)₄ that forms a trimeric helical bundle, with T-helper epitope underlined, and C-terminal a = d-alanine) and, iii V-306. Pam₂Cys is S-[R-2,3-bis(palmitoyloxy)propyl]-R-cysteine. b, left: Solution NMR structures of FsIIm. A superimposition of the final 20 structures is shown. Right: Superimposition of one typical NMR structure of FsIIm (green) and the Motavizumab antigen (orange) from PDB file 3IXT. c Schematic representation of the V-306 SVLP, formed by aggregation of trimeric coiled-coil V-306 lipopeptides (shown on the left, green ball = palivizumab epitope mimetic (V-306p), cylinder = helical coiled-coil domain, wavy line = Pam₂Cys lipid) into a ca. 25–30-nm diameter micelle-like nanoparticle (shown on the right).