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. 2017 Oct 13;7:13169. doi: 10.1038/s41598-017-13709-1

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© The Author(s) 2017

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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Binding of ATI-derived oligopeptides to surface-blocked TLR4. Superimposition of sensorgrams obtained at increasing concentrations of the straight peptide (RSGNVGESGLI, Panel A), and of the scrambled counterpart (SGIVLSGGRNE, Panel B). Competitive binding to TLR4 (Panel C). Comparison of binding of ATI to free surface-blocked TLR4, and upon pre-saturation of the receptor with RSGNVGESGLI (^#-marked curve) and with SGIVLSGGRNE (*-marked curve).