A Class of Disulfide Compounds Suppresses Ferroptosis by Stabilizing GPX4
Abstract
Ferroptosis is a nonapoptotic form of cell death characterized by iron-dependent lipid peroxidation and has been implicated in multiple pathological conditions. Glutathione peroxidase 4 (GPX4) plays an essential role in inhibiting ferroptosis by eliminating lipid peroxide using glutathione (GSH) as a reductant. In this study, we found Ellman's reagent DTNB and a series of disulfide compounds, including disulfiram (DSF), an FDA-approved drug, which protect cells from erastin-induced ferroptosis. Mechanistically, DTNB or DSF is conjugated to multiple cysteine residues in GPX4 and disrupts GPX4 interaction with HSC70, an adaptor protein for chaperone mediated autophagy, thus preventing GPX4 degradation induced by erastin. In addition, DSF ameliorates concanavalin A induced acute liver injury by suppressing ferroptosis in a mouse model. Our work reveals a novel regulatory mechanism for GPX4 protein stability control. We also discover disulfide compounds as a new class of ferroptosis inhibitors and suggest therapeutic repurposing of DSF in treating ferroptosis-related diseases.
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DIS suppresses ferroptosis by modifying cysteine residues on glutathione peroxidase 4, preventing its chaperone-mediated autophagic degradation; this stabilizes GPX4, enabling lipid peroxide detoxification and cytoprotection, as validated in the acute liver injury model.
“DIS suppresses ferroptosis by modifying cysteine residues on glutathione peroxidase 4 (GPX4), preventing its chaperone-mediated autophagic degradation. This stabilizes GPX4, enabling lipid peroxide detoxification and cytoprotection. The mechanism offers a novel approach to GPX4 regulation, with DIS showing repurposing potential in ferroptosis-driven diseases, as validated in the acute liver injury”
From Off-label and repurposed use of disulfiram beyond alcohol dependence: A systematic review of clinical and preclinical evidence (2026) · cites this paper as [119]
Cites
Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,383 · see citing works
Ferroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death
Dixon, S. J., Lemberg, K. M., Lamprecht, M. R., Skouta, R., Zaitsev, E. M., Gleason, C. E., Patel, D. N., Bauer, A. J., Cantley, A. M., Yang, W. S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.042 · Cited by 18,691 · see citing works
Regulation of Ferroptotic Cancer Cell Death by GPX4
Yang, W. S., SriRamaratnam, R., Welsch, M. E., Shimada, K., Skouta, R., Viswanathan, V. S., Cheah, J. H., Clemons, P. A., Shamji, A. F., Clish, C. B., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.010 · Cited by 7,713 · see citing works
Ferroptosis: mechanisms, biology and role in disease
Jiang, X., Stockwell, B. R., & Conrad, M. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00324-8 · Cited by 7,698 · see citing works
Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease
Stockwell, B. R., Friedmann Angeli, J. P., Bayir, H., Bush, A. I., Conrad, M., Dixon, S. J., Fulda, S., Gascón, S., Hatzios, S. K., Kagan, V. E., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.021 · Cited by 7,695 · see citing works
Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice
Friedmann Angeli, J. P., Schneider, M., Proneth, B., Tyurina, Y. Y., Tyurin, V. A., Hammond, V. J., Herbach, N., Aichler, M., Walch, A., Eggenhofer, E., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3064 · Cited by 3,732 · see citing works
Drug repositioning: identifying and developing new uses for existing drugs
Ashburn, T. T., & Thor, K. B. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1468 · Cited by 3,237 · see citing works
Oxidized arachidonic and adrenic PEs navigate cells to ferroptosis
Kagan, V. E., Mao, G., Qu, F., Angeli, J. P. F., Doll, S., Croix, C. S., Dar, H. H., Liu, B., Tyurin, V. A., Ritov, V. B., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2238 · Cited by 3,029 · see citing works
Peroxidation of polyunsaturated fatty acids by lipoxygenases drives ferroptosis
Yang, W. S., Kim, K. J., Gaschler, M. M., Patel, M., Shchepinov, M. S., & Stockwell, B. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603244113 · Cited by 2,329 · see citing works
The Metabolic Underpinnings of Ferroptosis
Zheng, J., & Conrad, M. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.10.011 · Cited by 1,338 · see citing works
Self-citationFDA-approved disulfiram inhibits pyroptosis by blocking gasdermin D pore formation
Hu, J. J., Liu, X., Xia, S., Zhang, Z., Zhang, Y., Zhao, J., Ruan, J., Luo, X., Lou, X., Bai, Y., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0669-6 · Cited by 1,145 · see citing works
Self-citationEnergy-stress-mediated AMPK activation inhibits ferroptosis
Lee, H., Zandkarimi, F., Zhang, Y., Meena, J. K., Kim, J., Zhuang, L., Tyagi, S., Ma, L., Westbrook, T. F., Steinberg, G. R., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0461-8 · Cited by 1,138 · see citing works
Tissue-specific functions of individual glutathione peroxidases
Brigelius-Flohé, R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00173-2 · Cited by 1,114 · see citing works
Global survey of cell death mechanisms reveals metabolic regulation of ferroptosis
Shimada, K., Skouta, R., Kaplan, A., Yang, W. S., Hayano, M., Dixon, S. J., Brown, L. M., Valenzuela, C. A., Wolpaw, A. J., & Stockwell, B. R. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2079 · Cited by 1,017 · see citing works
Transferrin Receptor Is a Specific Ferroptosis Marker
Feng, H., Schorpp, K., Jin, J., Yozwiak, C. E., Hoffstrom, B. G., Decker, A., Rajbhandari, P., Stokes, M. E., Bender, H. G., Csuka, J. M., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.049 · Cited by 891 · see citing works
Alcohol-abuse drug disulfiram targets cancer via p97 segregase adaptor NPL4
Skrott, Z., Mistrik, M., Andersen, K. K., Friis, S., Majera, D., Gursky, J., Ozdian, T., Bartkova, J., Turi, Z., Moudry, P., et al. (2017) · Nature · doi:10.1038/nature25016 · Cited by 807 · see citing works
Imai, H., & Nakagawa, Y. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01197-8 · Cited by 763 · see citing works
Yan, B., Ai, Y., Sun, Q., Ma, Y., Cao, Y., Wang, J., Zhang, Z., & Wang, X. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.024 · Cited by 651 · see citing works
Lipid Peroxidation-Dependent Cell Death Regulated by GPx4 and Ferroptosis
Imai, H., Matsuoka, M., Kumagai, T., Sakamoto, T., & Koumura, T. (2016) · Current topics in microbiology and immunology · doi:10.1007/82_2016_508 · Cited by 629 · see citing works
Chaperone-mediated autophagy is involved in the execution of ferroptosis
Wu, Z., Geng, Y., Lu, X., Shi, Y., Wu, G., Zhang, M., Shan, B., Pan, H., & Yuan, J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1819728116 · Cited by 582 · see citing works
Role of lipid peroxidation derived 4-hydroxynonenal (4-HNE) in cancer: Focusing on mitochondria
Zhong, H., & Yin, H. (2014) · Redox Biology · doi:10.1016/j.redox.2014.12.011 · Cited by 540 · see citing works
Mechanisms of Ferroptosis and Relations With Regulated Cell Death: A Review
Lei, P., Bai, T., & Sun, Y. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00139 · Cited by 535 · see citing works
Nagy, P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4973 · Cited by 488 · see citing works
Quantification of thiols and disulfides
Winther, J. R., & Thorpe, C. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.03.031 · Cited by 383 · see citing works
Cysteine Oxidative Posttranslational Modifications
Chung, H. S., Wang, S.-B., Venkatraman, V., Murray, C. I., & Eyk, J. E. V. (2013) · Circulation Research · doi:10.1161/circresaha.112.268680 · Cited by 297 · see citing works
Li, X., Wang, T., Huang, X., Li, Y., Sun, T., Zang, S., Guan, K., Xiong, Y., Liu, J., & Yuan, H. (2020) · Liver International · doi:10.1111/liv.14428 · Cited by 279 · see citing works
Self-citationDevelopment of small-molecule probes that selectively kill cells induced to express mutant RAS
Weïwer, M., Bittker, J. A., Lewis, T. A., Shimada, K., Yang, W. S., MacPherson, L., Dandapani, S., Palmer, M., Stockwell, B. R., Schreiber, S. L., et al. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.09.047 · Cited by 237 · see citing works
Human Aldehyde Dehydrogenase: Mechanism of Inhibition of Disulfiram
Vallari, R. C., & Pietruszko, R. (1982) · Science · doi:10.1126/science.7071604 · Cited by 235 · see citing works
The Expanding Landscape of the Thiol Redox Proteome
Yang, J. H., Carroll, K. S., & Liebler, D. C. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o115.056051 · Cited by 205 · see citing works
Cline, D. J., Redding, S. E., Brohawn, S. G., Psathas, J. N., Schneider, J. P., & Thorpe, C. (2004) · Biochemistry · doi:10.1021/bi048329a · Cited by 203 · see citing works
Shah, R., Margison, K. D., & Pratt, D. A. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00730 · Cited by 188 · see citing works
The combination of disulfiram and copper for cancer treatment
Li, H., Wang, J., Wu, C., Wang, L., Chen, Z.-S., & Cui, W. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.04.003 · Cited by 185 · see citing works
Disulfiram: a novel repurposed drug for cancer therapy
Chen, L., Li, X., Ren, Y., & Zhang, X. (2021) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-020-04216-8 · Cited by 159 · see citing works
Cvek, B. (2011) · Drug Discovery Today · doi:10.1016/j.drudis.2011.12.010 · Cited by 115 · see citing works
Characterization of a patient-derived variant of GPX4 for precision therapy
Liu, H., Forouhar, F., Seibt, T., Saneto, R. P., Wigby, K. M., Friedman, J., Xia, X., Shchepinov, M. S., Ramesh, S. K., Conrad, M., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00915-2 · Cited by 103 · see citing works
Viola-Rhenals, M., Patel, K., Laura, J.-S., Wu, G., Liu, J., & Dou, Q. P. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867324666171023161121 · Cited by 91 · see citing works
Self-citationHigh-throughput screening of small molecules identifies hepcidin antagonists
Fung, E., Sugianto, P., Hsu, J., Damoiseaux, R., Ganz, T., & Nemeth, E. (2013) · Molecular Pharmacology · doi:10.1124/mol.112.083428 · Cited by 78 · see citing works
Zeng, T., Deng, G., Zhong, W., Gao, Z., Ma, S., Mo, C., Li, Y., Huang, S., Zhou, C., Lai, Y., et al. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.01.009 · Cited by 71 · see citing works
Determination of in vivo adducts of disulfiram with mitochondrial aldehyde dehydrogenase
Shen, M. L., Johnson, K. L., Mays, D. C., Lipsky, J. J., & Naylor, S. (2001) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00586-4 · Cited by 57 · see citing works
Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infection
Stantchev, T. S., Paciga, M., Lankford, C. S. R., Schwartzkopff, F., Broder, C. C., & Clouse, K. A. (2012) · Retrovirology · doi:10.1186/1742-4690-9-97 · Cited by 41 · see citing works
Lee, S. A., Elliott, J., McMahon, J. H., Hartogenesis, W., Bumpus, N. N., Lifson, J. D., Gorelick, R. J., Bacchetti, P., Deeks, S. G., Lewin, S. R., et al. (2018) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.1220 · Cited by 39 · see citing works
Liegner, K. B. (2019) · Antibiotics · doi:10.3390/antibiotics8020072 · Cited by 35 · see citing works
Grant, G. A. (2017) · Current Protocols in Protein Science · doi:10.1002/cpps.22 · Cited by 16 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Chen, X., Tsvetkov, A. S., Shen, H., Isidoro, C., Ktistakis, N. T., Linkermann, A., Koopman, W. J. H., Simon, H., Galluzzi, L., Luo, S., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2319901 · Cited by 222 · see citing works
Self-citationTargeting GPX4 in human cancer: Implications of ferroptosis induction for tackling cancer resilience
Lee, J., & Roh, J. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216119 · Cited by 147 · see citing works
Ferroptosis inhibitors: past, present and future
Zhang, L., Luo, Y., Xiang, Y., Bai, X. Y., Qiang, R. R., Zhang, X., Yang, Y. L., & Liu, X. L. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1407335 · Cited by 103 · see citing works
Ferroptosis and Iron Homeostasis: Molecular Mechanisms and Neurodegenerative Disease Implications
Abdukarimov, N., Kokabi, K., & Kunz, J. (2025) · Antioxidants · doi:10.3390/antiox14050527 · Cited by 83 · see citing works
Ferroptosis inhibitors: mechanisms of action and therapeutic potential
Duo, K., Feng, X., Tian, X., Wang, F., Zhao, Y., Yu, J., Liu, Y., He, Y., & Cai, Z. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05958-5 · Cited by 48 · see citing works
Yang, W., Liu, R., Yin, X., Jin, Y., Wang, L., Dong, M., Wu, K., Yan, Z., Fan, G., Tang, Z., et al. (2023) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2023.134180 · Cited by 43 · see citing works
Zeng, C., Nie, D., Wang, X., Zhong, S., Zeng, X., Liu, X., Qiu, K., Peng, X., Zhang, W., Chen, S., et al. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02162-0 · Cited by 42 · see citing works
Zou, Y., Chen, J., Luo, X., Qu, Y., Zhou, M., Xia, R., Wang, W., & Zheng, X. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1481168 · Cited by 40 · see citing works
Ferroptosis-Based Therapeutic Strategies toward Precision Medicine for Cancer
Shi, T., Chen, X., & Ti, H. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01749 · Cited by 37 · see citing works
Research progress on GPX4 targeted compounds
Li, B., Cheng, K., Wang, T., Peng, X., Xu, P., Liu, G., Xue, D., Jiao, N., & Wang, C. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116548 · Cited by 34 · see citing works
Self-citationLin, H., Ji, F., Lin, K.-Q., Zhu, Y.-T., Yang, W., Zhang, L.-H., Zhao, J.-G., & Pei, Y. (2023) · Inflammation · doi:10.1007/s10753-023-01804-7 · Cited by 31 · see citing works
Decoding GPX4 regulation in ferroptosis: mechanisms and therapeutic implications
Chen, X. (2026) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2026.01.008 · Cited by 25 · see citing works
Targeting ferroptosis and ferritinophagy: new targets for cardiovascular diseases
Luan, Y., Yang, Y., Luan, Y., Liu, H., Han, X., Pei, J., Liu, H., Qin, B., & Ren, K. (2024) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2300097 · Cited by 16 · see citing works
Research progress of ferroptosis and inflammatory bowel disease
Ma, B., Hu, X., Ai, X., & Zhang, Y. (2024) · BioMetals · doi:10.1007/s10534-024-00604-2 · Cited by 13 · see citing works
Ferroptosis: A new way to intervene in the game between Mycobacterium tuberculosis and macrophages
Jumabayi, W., Reyimu, A., Zheng, R., Paerhati, P., Rahman, M., Zou, X., & Xu, A. (2024) · Microbial Pathogenesis · doi:10.1016/j.micpath.2024.107014 · Cited by 12 · see citing works
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Zhang, J., Lin, F., Xiao, Y., Cen, S.-Y., Wan, B.-W., Li, X., Zhao, Y., He, Y., Yuan, H., & Nie, S. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117192 · Cited by 10 · see citing works
Self-citationLin, W., Li, H., Chang, J., & Huang, Y. (2024) · Gene · doi:10.1016/j.gene.2024.148944 · Cited by 8 · see citing works
Double-edged sword effect of GPX4 in skin homeostasis and diseases
Xu, H., Li, Y., Wu, Y., & Lei, H. (2025) · Archives of Dermatological Research · doi:10.1007/s00403-025-03903-x · Cited by 7 · see citing works
Discovery of novel benzo[b][1,4]oxazine derivatives as ferroptosis inhibitors
Wan, B.-W., Liu, W., Xiao, Y., Lv, L., Li, X., Lin, F., Zhao, Y., He, Y., Nie, S., Yang, X., et al. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108201 · Cited by 5 · see citing works
Self-citationYou, J., Yang, L., Qin, Y., Tian, C., Yang, X., Xiang, M., Li, L., & Yang, S. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02855 · Cited by 3 · see citing works
Lp‑PLA2 in the cancer landscape: From molecular mechanisms to therapeutic potential (Review)
Yang, X., Tu, Y., Liang, N., Li, L., Zhang, J., Xu, J., & Li, C. (2025) · International Journal of Oncology · doi:10.3892/ijo.2025.5793 · Cited by 2 · see citing works
Wang, C., & Wang, S. (2024) · Cell investigation. · doi:10.1016/j.clnves.2024.100006 · Cited by 2 · see citing works
Benkő, B.-M., De Brito Parreirinha, N. S., Sebe, I., & Zelkó, R. (2026) · iScience · doi:10.1016/j.isci.2026.115441 · Cited by 2 · see citing works
Tiek, D. M., Song, X., Wu, R., Yu, X., Walker, M. N., Mao, Y., Sisbarro, D., He, Q. Q., Magassa, A., Singh, A., et al. (2025) · Neuro-Oncology · doi:10.1093/neuonc/noaf265 · Cited by 1 · see citing works
Liu, R., Zhang, Y., Zou, H., Zhang, M. H., Yang, Z., Liao, K., Wang, G., Liu, B., Tang, L., Kang, X., et al. (2026) · Pharmaceutical Biology · doi:10.1080/13880209.2026.2646350 · Cited by 1 · see citing works
Deng, L., Liu, K., Peng, J., & Luo, L. (2026) · Medicinal Research Reviews · doi:10.1002/med.70099 · Cited by 1 · see citing works
Vichova, T., & Motovska, Z. J. (2025) · Thrombosis and Haemostasis · doi:10.1055/a-2741-4754
Effect of Betulinic Acid on GPX4 and SLC7A11 Gene Expression in Renal Cell Carcinoma Cell Line
İlvan, L. A., Kuraş, S., Ataş, M. N., & Ergen, A. (2026) · Hitit Medical Journal · doi:10.52827/hititmedj.1730449
BindingDB Entry 50022029: Research progress on GPX4 targeted compounds.
BindingDB (2025) · UC San Diego · doi:10.7270/q2z03dt5
- Authors
- Liu, J.-P., Cen, S.-Y., Xue, Z., Wang, T.-X., Gao, Y., Zheng, J., Zhang, C., Hu, J., Nie, S., Xiong, Y., Guan, K.-L., & Yuan, H.-X.
- Affiliations
- Shanghai Medical College of Fudan University (CN)
- The Fifth People’s Hospital of Shanghai, Molecular and Cell Biology Laboratory, Institutes of Biomedical Sciences and the School of Pharmacy, Fudan University, Shanghai200032, China
- Chongqing Medical University (CN)
- Cullgen Inc., 12671 High Bluff Drive, San Diego, California92130, United States
- University of California San Diego (US)
- Corresponding author
- Yuan, Hai-Xin
- ORCID
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2022-11-29
- Volume
- 17
- Issue
- 12
- Pages
- 3389-3406
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- OpenAlex
- W4310462660
- Cited by
- 29
- References
- 43
- Citations by year
- 2026: 6 · 2025: 8 · 2024: 12 · 2023: 3
- FWCI
- 3.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- ACS Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Science and Technology of the People's Republic of China (2018YFA0800304)
- Venture and Innovation Support Program for Chongqing Overseas Returnees (cx2022012)
- National Natural Science Foundation of China (31970684)
- Development Fund for Shanghai Talents (2019109)
- Topics
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- ferroptosis, GPX4, disulfides, disulfiram, DTNB, erastin, Hsc70, chaperone-mediated autophagy, lipid peroxidation, acute liver injury, concanavalin A, drug repurposing, ferroptosis inhibitors
- MeSH terms
- Ferroptosis, Phospholipid Hydroperoxide Glutathione Peroxidase, Animals, Disulfides, Disulfiram, Dithionitrobenzoic Acid, Glutathione, Sulfides, Lipid Peroxidation, Mice
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