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. 2017 Jun 21;7:3945. doi: 10.1038/s41598-017-04233-3

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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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Effect of chlorophyllin sodium copper salt and bonaphton on binding of Keap1 to Nrf2. To clarify that (A) chlorophyllin sodium copper salt, and (B) bonaphton disrupt the interaction between Keap1 and Nrf2 by an alternative experiment other than FCS, we performed co-immunoprecipitation assay for the verification of disruption of Keap1 interaction by these compounds. BioEase-tagged Nrf2 was successfully immunoprecipitated by Halo-tagged Keap1, using Halo-antibody. Both of the compounds induced consistent decrease in binding between the two proteins, although protein-protein interaction between Keap1 and Nrf2 was not decreased by sulforaphane that does not disrupt interaction between Keap1 and Nrf2. This result indicated that these compounds inhibited the Keap1-Nrf2 protein-protein interactions directly. Experiments were repeated three times with consistent results, and a representative blot is shown. Full-length blots are presented in Supplementary Fig. S3.