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Open AccessArticle

Probing the Interactions of Ochratoxin B, Ochratoxin C, Patulin, Deoxynivalenol, and T-2 Toxin with Human Serum Albumin

1
Department of Pharmacology, Faculty of Pharmacy, University of Pécs, Szigeti út 12, H-7624 Pécs, Hungary
2
János Szentágothai Research Centre, Ifjúság útja 20, H-7624 Pécs, Hungary
3
Institute of Organic and Medicinal Chemistry, Medical School, University of Pécs, Szigeti út 12, H-7624 Pécs, Hungary
4
Department of Laboratory Medicine, University of Pécs, Medical School, Ifjúság útja 13, H-7624 Pécs, Hungary
5
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar Tudósok krt. 2, H-1117 Budapest, Hungary
*
Author to whom correspondence should be addressed.
Toxins 2020, 12(6), 392; https://doi.org/10.3390/toxins12060392
Received: 19 May 2020 / Revised: 8 June 2020 / Accepted: 10 June 2020 / Published: 13 June 2020
(This article belongs to the Section Mycotoxins)
Ochratoxins, patulin, deoxynivalenol, and T-2 toxin are mycotoxins, and common contaminants in food and drinks. Human serum albumin (HSA) forms complexes with certain mycotoxins. Since HSA can affect the toxicokinetics of bound ligand molecules, the potential interactions of ochratoxin B (OTB), ochratoxin C (OTC), patulin, deoxynivalenol, and T-2 toxin with HSA were examined, employing spectroscopic (fluorescence, UV, and circular dichroism) and ultrafiltration techniques. Furthermore, the influence of albumin on the cytotoxicity of these xenobiotics was also evaluated in cell experiments. Fluorescence studies showed the formation of highly stable OTB–HSA and OTC–HSA complexes. Furthermore, fluorescence quenching and circular dichroism measurements suggest weak or no interaction of patulin, deoxynivalenol, and T-2 toxin with HSA. In ultrafiltration studies, OTB and OTC strongly displaced the Sudlow’s site I ligand warfarin, while other mycotoxins tested did not affect either the albumin binding of warfarin or naproxen. The presence of HSA significantly decreased or even abolished the OTB- and OTC-induced cytotoxicity in cell experiments; however, the toxic impacts of patulin, deoxynivalenol, and T-2 toxin were not affected by HSA. In summary, the complex formation of OTB and OTC with albumin is relevant, whereas the interactions of patulin, deoxynivalenol, and T-2 toxin with HSA may have low toxicological importance. View Full-Text
Keywords: ochratoxin B; ochratoxin C; patulin; deoxynivalenol; T-2 toxin; human serum albumin; fluorescence spectroscopy; optical spectroscopy; albumin–ligand interaction; cytotoxicity ochratoxin B; ochratoxin C; patulin; deoxynivalenol; T-2 toxin; human serum albumin; fluorescence spectroscopy; optical spectroscopy; albumin–ligand interaction; cytotoxicity
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Faisal, Z.; Vörös, V.; Fliszár-Nyúl, E.; Lemli, B.; Kunsági-Máté, S.; Csepregi, R.; Kőszegi, T.; Zsila, F.; Poór, M. Probing the Interactions of Ochratoxin B, Ochratoxin C, Patulin, Deoxynivalenol, and T-2 Toxin with Human Serum Albumin. Toxins 2020, 12, 392.

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