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Article

Interaction of the Emerging Mycotoxins Beauvericin, Cyclopiazonic Acid, and Sterigmatocystin with Human Serum Albumin

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Department of Pharmacology, Faculty of Pharmacy, University of Pécs, Rókus u. 2, H-7624 Pécs, Hungary
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Food Biotechnology Research Group, János Szentágothai Research Centre, University of Pécs, Ifjúság útja 20, H-7624 Pécs, Hungary
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Department of Organic and Pharmacological Chemistry, Faculty of Pharmacy, University of Pécs, Szigeti út 12, H-7624 Pécs, Hungary
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Green Chemistry Research Group, János Szentágothai Research Centre, University of Pécs, Ifjúság útja 20, H-7624 Pécs, Hungary
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Pharmacoinformatics Unit, Department of Pharmacology and Pharmacotherapy, Medical School, University of Pécs, Szigeti út 12, H-7624 Pécs, Hungary
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Institute of Physiology and Nutrition, Department of Physiology and Animal Health, Agribiotechnology and Precision Breeding for Food Security National Laboratory, Hungarian University of Agriculture and Life Sciences, H-2103 Gödöllő, Hungary
*
Author to whom correspondence should be addressed.
Academic Editor: Hang Fai Kwok
Biomolecules 2022, 12(8), 1106; https://doi.org/10.3390/biom12081106
Received: 11 July 2022 / Revised: 8 August 2022 / Accepted: 10 August 2022 / Published: 11 August 2022
Beauvericin (BEA), cyclopiazonic acid (CPA), and sterigmatocystin (STC) are emerging mycotoxins. They appear as contaminants in food and animal feed, leading to economic losses and health risks. Human serum albumin (HSA) forms stable complexes with certain mycotoxins, including ochratoxins, alternariol, citrinin, and zearalenone. HSA binding can influence the toxicokinetics of xenobiotics, and albumin can also be considered and applied as a relatively cheap affinity protein. Therefore, we examined the potential interactions of BEA, CPA, and STC with HSA employing fluorescence spectroscopy, ultracentrifugation, ultrafiltration, and molecular modeling. Spectroscopic and ultracentrifugation studies demonstrated the formation of low-affinity BEA–HSA (Ka ≈ 103 L/mol) and moderately strong CPA–HSA and STC–HSA complexes (Ka ≈ 104 L/mol). In ultrafiltration experiments, CPA slightly displaced each site marker (warfarin, naproxen, and camptothecin) tested, while BEA and STC did not affect significantly the albumin binding of these drugs. Modeling studies suggest that CPA occupies Sudlow’s site I, while STC binds to the Heme site (FA1) on HSA. Considering the interactions of CPA with the site markers, the CPA–HSA interaction may have toxicological importance. View Full-Text
Keywords: beauvericin; cyclopiazonic acid; sterigmatocystin; human serum albumin; albumin–ligand interaction beauvericin; cyclopiazonic acid; sterigmatocystin; human serum albumin; albumin–ligand interaction
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MDPI and ACS Style

Fliszár-Nyúl, E.; Faisal, Z.; Skaper, R.; Lemli, B.; Bayartsetseg, B.; Hetényi, C.; Gömbös, P.; Szabó, A.; Poór, M. Interaction of the Emerging Mycotoxins Beauvericin, Cyclopiazonic Acid, and Sterigmatocystin with Human Serum Albumin. Biomolecules 2022, 12, 1106. https://doi.org/10.3390/biom12081106

AMA Style

Fliszár-Nyúl E, Faisal Z, Skaper R, Lemli B, Bayartsetseg B, Hetényi C, Gömbös P, Szabó A, Poór M. Interaction of the Emerging Mycotoxins Beauvericin, Cyclopiazonic Acid, and Sterigmatocystin with Human Serum Albumin. Biomolecules. 2022; 12(8):1106. https://doi.org/10.3390/biom12081106

Chicago/Turabian Style

Fliszár-Nyúl, Eszter, Zelma Faisal, Renáta Skaper, Beáta Lemli, Bayarsaikhan Bayartsetseg, Csaba Hetényi, Patrik Gömbös, András Szabó, and Miklós Poór. 2022. "Interaction of the Emerging Mycotoxins Beauvericin, Cyclopiazonic Acid, and Sterigmatocystin with Human Serum Albumin" Biomolecules 12, no. 8: 1106. https://doi.org/10.3390/biom12081106

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