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. 2022 Sep 26;18(11):1184–1195. doi: 10.1038/s41589-022-01116-1

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© The Author(s) 2022

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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Extended Data Fig. 9 — Compounds were evaluated for their ability to be hydrolyzed from di-ester to mono-ester, or to di-acid CypD inhibitors. Each reaction was analyzed by LC-MS, and ion abundances for each are shown as a percent of the total sum. These were conducted under conditions of: a, Tris-HCl buffer only; b, 250 nM carboxylesterase 1 (CES1); c, 250 nM carboxylesterase 2 (CES2); d, incubated with A549 cells for 48 h and intracellular fraction isolated; e, incubated with HeLa cells for 48 h and intracellular fraction isolated; f, incubated with HEK293T cells for 48 h and intracellular fraction isolated; g, incubated with MEFs for 48 h and intracellular fraction isolated; h, incubated with HepG2 cells for 36 h and intracellular fraction isolated. Esters show good stability in buffer and are only cleaved under esterase conditions, or intracellularly, with B52-Et-Cy5 showing the most rapidly hydrolyzed esters. Values and error bars reflect mean ± s.d. of three technical replicates.

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