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. 2019 Feb 19;9:2317. doi: 10.1038/s41598-018-36492-z

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© The Author(s) 2019

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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SPR analysis for KCF18 binding to proinflammatory cytokines. (A) KCF18 was injected over TNF-α immobilized on the CM5 sensor chip. As the concentration of KCF18 increased, the measured response for the binding of KCF18 to TNF-α also increased, indicating that binding was concentration dependent. (B) For the steady–state interaction, a binding isotherm was generated to determine the equilibrium K_D and R_max for the binding of KCF18 to cytokine TNF-α, which were found to be 60.9 μM and 197.1 RU, respectively. (C) KCF18 was injected over IL-6 immobilized on the CM5 sensor chip. The measured response for the binding of KCF18 to IL-6 also increased with the concentration of KCF18, similar to the profile of the binding of KCF18 to TNF-α. (D) The kinetic analysis of binding isotherm was also performed to determine the equilibrium dissociation K_D and R_max for KCF18 binding to cytokine IL-6, which were found to be 111.5 μM and 210.3 RU, respectively.