ArticleMycotoxin research2018
Interactions of zearalenone and its reduced metabolites α-zearalenol and β-zearalenol with serum albumins: species differences, binding sites, and thermodynamics.
Article in Mycotoxin research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
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- Simultaneous binding characterization of different chromium speciation to serum albumin.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
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- Interaction of the Emerging Mycotoxins Beauvericin, Cyclopiazonic Acid, and Sterigmatocystin with Human Serum Albumin.Biomolecules · 2022Article
- In vitro characterization of the furin inhibitor MI-1851: Albumin binding, interaction with cytochrome P450 enzymes and cytotoxicity.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022Article
- In vitro interaction of potential antiviral TMPRSS2 inhibitors with human serum albumin and cytochrome P 450 isoenzymes.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022Article
- Effects of Microenvironmental Changes on the Fluorescence Signal of Alternariol: Magnesium Induces Strong Enhancement in the Fluorescence of the Mycotoxin.International journal of molecular sciences · 2021Article
- In Vitro Evaluation of the Individual and Combined Cytotoxic and Estrogenic Effects of Zearalenone, Its Reduced Metabolites, Alternariol, and Genistein.International journal of molecular sciences · 2021Article
- Interactions of zearalanone, α-zearalanol, β-zearalanol, zearalenone-14-sulfate, and zearalenone-14-glucoside with serum albumin.Mycotoxin research · 2020Article
- Article
- Zearalenone (ZEN) in Livestock and Poultry: Dose, Toxicokinetics, Toxicity and Estrogenicity.Toxins · 2020Review
- Testing the Pharmacokinetic Interactions of 24 Colonic Flavonoid Metabolites with Human Serum Albumin and Cytochrome P450 Enzymes.Biomolecules · 2020Article
- Article
- Interaction of Mycotoxin Alternariol with Serum Albumin.International journal of molecular sciences · 2019Article
- Interaction of the mycotoxin metabolite dihydrocitrinone with serum albumin.Mycotoxin research · 2019Article
- Article
- Interaction of Chrysin and Its Main Conjugated Metabolites Chrysin-7-Sulfate and Chrysin-7-Glucuronide with Serum Albumin.International journal of molecular sciences · 2018Article
- Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Zearalenone (ZEN) is a mycotoxin produced by Fusarium species. ZEN mainly appears in cereals and related foodstuffs, causing reproductive disorders in animals, due to its xenoestrogenic effects. The main reduced metabolites of ZEN are α-zearalenol (α-ZEL) and β-zearalenol (β-ZEL). Similarly to ZEN, ZELs can also activate estrogen receptors; moreover, α-ZEL is the most potent endocrine disruptor among these three compounds. Serum albumin is the most abundant plasma protein in the circulation; it affects the tissue distribution and elimination of several drugs and xenobiotics. Although ZEN binds to albumin with high affinity, albumin-binding of α-ZEL and β-ZEL has not been investigated. In this study, the complex formation of ZEN, α-ZEL, and β-ZEL with human (HSA), bovine (BSA), porcine (PSA), and rat serum albumins (RSA) was investigated by fluorescence spectroscopy, affinity chromatography, thermodynamic studies, and molecular modeling. Our main observations are as follows: (1) ZEN binds with higher affinity to albumins than α-ZEL and β-ZEL. (2) The low binding affinity of β-ZEL toward albumin may result from its different binding position or binding site. (3) The binding constants of the mycotoxin-albumin complexes significantly vary with the species. (4) From the thermodynamic point of view, the formation of ZEN-HSA and ZEN-RSA complexes are similar, while the formation of ZEN-BSA and ZEN-PSA complexes are markedly different. These results suggest that the toxicological relevance of ZEN-albumin and ZEL-albumin interactions may also be species-dependent.
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