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. 2017 Nov 6;7:14514. doi: 10.1038/s41598-017-15108-y

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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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Identification of thiostrepton as a claudin-4 binder. (a) Results of the TR-FRET-based high-throughput screening for claudin-4 binders. (b) Inhibition of the interaction between claudin-4 and C-CPE by thiostrepton in the TR-FRET assay. Thiostrepton was assayed in triplicate at various concentrations (1 nM to 10 μM) to assess its inhibitory effect. Data are means ± SD (n = 3). IC₅₀, concentration at which the inhibitory response was reduced to 50%. (c) Competition assay of the interaction of thiostrepton with claudin-3 and claudin-4. Claudin-3- or claudin-4-expressing HT1080 cells (HT1080/CLDN3 or HT1080/CLDN4) and control (claudin non-expressing) HT1080 cells (HT1080/vector) were treated with vehicle alone, 10 µg/mL BSA or 10 µg/mL BSA plus 1 mM thiostrepton for 1 h. Then, FITC-conjugated C-CPE was added to the cells at 20 µg/mL for 1 h. The thiostrepton-bound cells were used for fluorescence-activated cell sorting analysis. Results for cells treated with vehicle alone are displayed in black. Results for cells treated with BSA with or without thiostrepton are displayed in grey or white, respectively.