Potent inhibition of human and rat 17β-hydroxysteroid dehydrogenase 1 by curcuminoids and the metabolites: 3D QSAR and in silico docking analysis

J He, Z Ji, J Sang, H Quan, H Zhang, H Lu, J Zheng, S Wang, R S Ge, X Li
SAR and QSAR in environmental research · 2024 · vol. 35(6) , pp. 433–456 · doi:10.1080/1062936X.2024.2355529 · PMID:38785078
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⚙ AI-generated summary by claude@2026-06, 2026-06-08 ⓘ

Curcuminoids and their metabolites, including demethoxycurcumin and dihydrocurcumin, were found to potently inhibit human and rat 17β-HSD1 enzyme activity, suppressing estradiol secretion and interacting with steroid or NADPH/steroid binding sites.

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The paper studied whether curcuminoids, their metabolites, and analogues inhibit human and rat 17β-hydroxysteroid dehydrogenase 1 (17β-HSD1), an enzyme involved in oestradiol production, using enzymatic screening of 10 compounds and cell assays in human BeWo cells. Demethoxycurcumin (IC50 3.97 μM) and dihydrocurcumin (IC50 5.84 μM) showed varying inhibitory potency, and compounds suppressed oestradiol secretion in BeWo cells at concentrations ≥5–10 μM, while 3D-QSAR and in silico docking (including Gromacs simulations) indicated competitive or mixed binding to steroid or NADPH/steroid binding sites, with hydrophobic regions and hydrogen bonding important for activity. A key limitation is that the mechanistic conclusions rely on computational docking/QSAR and the cell system used is not a direct endometriosis or adenomyosis model. Relevance to endometriosis: the authors state that 17β-HSD1 has significant involvement in endometriosis, though the study’s main focus is inhibitory effects and modeling of curcuminoids on 17β-HSD1 rather than direct endometriosis experimentation.

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Abstract

Curcumin, an extensively utilized natural pigment in the food industry, has attracted considerable attention due to its potential therapeutic effects, such as anti-tumorigenic and anti-inflammatory activities. The enzyme 17β-Hydroxysteroid dehydrogenase 1 (17β-HSD1) holds a crucial position in oestradiol production and exhibits significant involvement in oestrogen-responsive breast cancers and endometriosis. This study investigated the inhibitory effects of curcuminoids, metabolites, and analogues on 17β-HSD1, a key enzyme in oestradiol synthesis. Screening 10 compounds, including demethoxycurcumin (IC50, 3.97 μM) and dihydrocurcumin (IC50, 5.84 μM), against human and rat 17β-HSD1 revealed varying inhibitory potencies. These compounds suppressed oestradiol secretion in human BeWo cells at ≥ 5-10 μM. 3D-Quantitative structure-activity relationship (3D-QSAR) and molecular docking analyses elucidated the interaction mechanisms. Docking studies and Gromacs simulations suggested competitive or mixed binding to the steroid or NADPH/steroid binding sites of 17β-HSD1. Predictive 3D-QSAR models highlighted the importance of hydrophobic regions and hydrogen bonding in inhibiting 17β-HSD1 activity. In conclusion, this study provides valuable insights into the inhibitory effects and mode of action of curcuminoids, metabolites, and analogues on 17β-HSD1, which may have implications in the field of hormone-related disorders.
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Abstract

Curcumin, an extensively utilized natural pigment in the food industry, has attracted considerable attention due to its potential therapeutic effects, such as anti-tumorigenic and anti-inflammatory activities. The enzyme 17β-Hydroxysteroid dehydrogenase 1 (17β-HSD1) holds a crucial position in oestradiol production and exhibits significant involvement in oestrogen-responsive breast cancers and endometriosis. This study investigated the inhibitory effects of curcuminoids, metabolites, and analogues on 17β-HSD1, a key enzyme in oestradiol synthesis. Screening 10 compounds, including demethoxycurcumin (IC50, 3.97 μM) and dihydrocurcumin (IC50, 5.84 μM), against human and rat 17β-HSD1 revealed varying inhibitory potencies. These compounds suppressed oestradiol secretion in human BeWo cells at ≥ 5–10 μM. 3D-Quantitative structure-activity relationship (3D-QSAR) and molecular docking analyses elucidated the interaction mechanisms. Docking studies and Gromacs simulations suggested competitive or mixed binding to the steroid or NADPH/steroid binding sites of 17β-HSD1. Predictive 3D-QSAR models highlighted the importance of hydrophobic regions and hydrogen bonding in inhibiting 17β-HSD1 activity. In conclusion, this study provides valuable insights into the inhibitory effects and mode of action of curcuminoids, metabolites, and analogues on 17β-HSD1, which may have implications in the field of hormone-related disorders.

Acknowledgements

We declare that we have no financial and personal relationships with other people or organizations that can inappropriately influence our work, there is no professional or other personal interest of any nature or kind in any product, service and/or company that could be construed as influencing the position presented in, or the review of, the manuscript entitled. Disclosure statement No potential conflict of interest was reported by the author(s). Ethics approval and consent to participate Term human placenta was obtained from the Second Affiliated Hospital of Wenzhou Medical University and used under the guidance of the Clinical Research Committee of Wenzhou Medical University (Protocol no. 2022-K-81-01). Supplementary material Supplemental data for this article can be accessed at: https://doi.org/10.1080/1062936X.2024.2355529.

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Condition tags

endometriosis

MeSH descriptors

17-Hydroxysteroid Dehydrogenases 17-Hydroxysteroid Dehydrogenases 17-Hydroxysteroid Dehydrogenases 17-Hydroxysteroid Dehydrogenases 17-Hydroxysteroid Dehydrogenases 17-Hydroxysteroid Dehydrogenases 17-Hydroxysteroid Dehydrogenases 17-Hydroxysteroid Dehydrogenases Curcumin Curcumin Curcumin Curcumin Curcumin Curcumin Curcumin Curcumin Curcumin Molecular Docking Simulation Molecular Docking Simulation Molecular Docking Simulation

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