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. 2017 Jul 26;7:6607. doi: 10.1038/s41598-017-06993-4

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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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Dodecameric TNF muteins have higher affinity to TNFR2 Binding of oligomerized TNF muteins to mouse TNFR2 was analyzed by QCM at high (A; 270 Hz) and low (B; 130 Hz) density of immobilized mouse TNFR2-Fc. Oligomerized TNF muteins were analyzed at concentrations between 2–32 nM (A) or 8–256 nM (B) at 37 °C in triplicates for each concentration (dashed lines = data curves, solid lines = fitted curves).