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. 2020 Jan 28;10:1290. doi: 10.1038/s41598-020-57940-9

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© The Author(s) 2020

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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Cucurbitacin B and I bind to Notch-1 protein. (A) Binding of C-B and C-I in the protein cavity of Notch ankyrin domains was assessed by molecular docking technique. C-B and C-I bind to the protein with the binding energy (B.E.) of −6.8 and −7.5 Kcal/mol respectively. Cartoon and surface models are shown in the figure for C-B (A and B) and C-I (C and D) respectively. (B) The docking results and consensus scores of C-B and C-I binding to Notch ankyrin domains are summarized. (C) Cellular thermal shift assay (CETSA) shows stabilization of Notch-1 protein after in the presence of C-B and C-I suggesting the potential binding. C-B and C-I were incubated with cell lysates from SW480 cell lines for two hours then subjected to thermal denaturation and evaluated using western blot. (D) Results from densitometric evaluation of CETSA assays. Notch-1 levels are represented relative to the band at 54 °C.