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. 2017 Oct 6;7:12758. doi: 10.1038/s41598-017-12630-x

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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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Biochemical characterization of mIDH1 inhibitors. (A) Scheme of IDH1 and mIDH1 enzymatic reactions coupled to diaphorase for fluorescence detection. B-D, Dose-response analyses show the selectivity of mIDH1 inhibitors on the activity of purified (B) wild type IDH1, (C) R132H and (D) R132C mIDH1 enzymes (n = 3). (E) Comparison of mIDH1 inhibitors Log IC₅₀ values on the activity of R132H and R132C mIDH1 enzymes show a strong correlation (R² = 0.85, P value = 0.001). A large dose-response shift is shown for (F) ML309 compared to (G) Novartis 530 when using a range of concentrations of α-KG, suggesting ML309 acts as a competitive inhibitor (n = 3).