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. 2022 Mar 7;13:817596. doi: 10.3389/fphar.2022.817596

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Copyright © 2022 Yuan, Hu, Liu, Xie, Yang, Li, Zhang, Chen, Tang and Shen.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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DCL directly interacts with IKKα/β and Keap1 respectively. The effects of DCL on the thermal stability of IKKα/β (A, upper panel) and Keap1 (D, upper panel) were analyzed by CETSA coupling western blotting assay. The CETSA curves of IKKα/β (A, bottom panel) and Keap1 (D, bottom panel) were shown. The densitometries of IKKα/β and Keap1 were normalized with respect to those obtained at 45°C. The effects of DCL on the protein’s proteolytic susceptibility of IKKα/β (B, upper panel) and Keap1 (E, upper panel) were analyzed by DARTS assay. The densitometry analysis of IKKα/β (B, bottom panel) and Keap1 (E, bottom panel) were shown. Molecular docking of DCL with IKKβ (C, PDB: 3QA8) and Keap1 (F, PDB: 4CXI). The covalent bonds are shown in purple. Data are represented as mean ± SEM, n = 3. ^* p < 0.05, ^** p < 0.01, ^*** p < 0.001, ^**** p < 0.0001.