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. 2020 Oct 1;3:547. doi: 10.1038/s42003-020-01266-9

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© The Author(s) 2020

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 Crystal structure of the Lpp trimer (PDB code, 1EQ7; cartoon presentation) with a close-up view of the C-terminal region. All Tyr56 (cyan sticks) and Arg57 (magenta sticks) residues roughly sit in the same plane. Distances from the center to the Tyr56-Cα and Arg57-Cα are 5.0 Å and 7.3 Å, respectively. b Synthesis of the tripodal peptidyl compounds, TMB_(Cys_peptide). Peptides are attached to the benzyl positions of 1,3,5-trimethylbenzene (TMB) via the N-terminal cysteine. Distance from the center to the cysteine-Cα in the extended tripodal compound is about 6.7 Å.