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. 2024 Jan 19;14:1739. doi: 10.1038/s41598-023-50964-x

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Kinetics of EZH2 binding by pyridone-based active site inhibitors. (a) Structural features of the EZH2 inhibitor set investigated in this study. All compounds share a common pyridone motif in the north side of the molecule and are differentiated by distinct chemical cores highlighted in different colors. For two of the Bayer-proprietary chemical series, distinctive colors were only applied to label the linkage between the pyridone and the undisclosed heterocyclic scaffolds. Whenever relevant (and feasible), this color code was subsequently used to label compounds throughout the entire paper. (b) Rate plots with isoaffinity diagonals (RAPID) representing the binding to wild type and mutant EZH2 of all compounds investigated in this study. Compounds are colored and numbered as in panel a for visualization of structure kinetic relationships (SKR). Open or filled symbols represent data generated in the absence or presence of H3K27me3 peptide.