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Toxins 2018, 10(9), 353; https://doi.org/10.3390/toxins10090353

Interaction of 2′R-ochratoxin A with Serum Albumins: Binding Site, Effects of Site Markers, Thermodynamics, Species Differences of Albumin-binding, and Influence of Albumin on Its Toxicity in MDCK Cells

1
Department of Pharmacology, Faculty of Pharmacy, University of Pécs, Szigeti út 12, H-7624 Pécs, Hungary
2
János Szentágothai Research Center, University of Pécs, Ifjúság útja 20, H-7624 Pécs, Hungary
3
Department of General and Physical Chemistry, University of Pécs, Ifjúság útja 6, H-7624 Pécs, Hungary
4
Department of Pharmaceutical Chemistry, Faculty of Pharmacy, University of Pécs, Rókus u. 2, H-7624 Pécs, Hungary
5
Department of Pharmacology and Pharmacotherapy, Medical School, University of Pécs, Szigeti út 12, H-7624 Pécs, Hungary
6
Department of Laboratory Medicine, Medical School, University of Pécs, Ifjúság útja 13, H-7624 Pécs, Hungary
7
Institute of Food Chemistry, Westfälische Wilhelms-Universität Münster, Corrensstr. 45, 48149 Münster, Germany
*
Author to whom correspondence should be addressed.
Received: 18 July 2018 / Revised: 17 August 2018 / Accepted: 27 August 2018 / Published: 1 September 2018
(This article belongs to the Collection Ochratoxins-Collection)
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Abstract

Ochratoxin A (OTA) is a nephrotoxic mycotoxin. Roasting of OTA-contaminated coffee results in the formation of 2′R-ochratoxin A (2′R-OTA), which appears in the blood of coffee drinkers. Human serum albumin (HSA) binds 2′R-OTA (and OTA) with high affinity; therefore, albumin may influence the tissue uptake and elimination of ochratoxins. We aimed to investigate the binding site of 2′R-OTA (verses OTA) in HSA and the displacing effects of site markers to explore which molecules can interfere with its albumin-binding. Affinity of 2′R-OTA toward albumins from various species (human, bovine, porcine and rat) was tested to evaluate the interspecies differences regarding 2′R-OTA-albumin interaction. Thermodynamic studies were performed to give a deeper insight into the molecular background of the complex formation. Besides fluorescence spectroscopic and modeling studies, effects of HSA, and fetal bovine serum on the cytotoxicity of 2′R-OTA and OTA were tested in MDCK kidney cell line in order to demonstrate the influence of albumin-binding on the cellular uptake of ochratoxins. Site markers displaced more effectively 2′R-OTA than OTA from HSA. Fluorescence and binding constants of 2′R-OTA-albumin and OTA-albumin complexes showed different tendencies. Albumin significantly decreased the cytotoxicity of ochratoxins. 2′R-OTA, even at sub-toxic concentrations, increased the toxic action of OTA. View Full-Text
Keywords: 2′R-ochratoxin A; ochratoxin A; serum albumin; albumin-ligand interaction; species differences; cellular toxicity 2′R-ochratoxin A; ochratoxin A; serum albumin; albumin-ligand interaction; species differences; cellular toxicity
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Faisal, Z.; Derdák, D.; Lemli, B.; Kunsági-Máté, S.; Bálint, M.; Hetényi, C.; Csepregi, R.; Kőszegi, T.; Sueck, F.; Cramer, B.; Humpf, H.-U.; Poór, M. Interaction of 2′R-ochratoxin A with Serum Albumins: Binding Site, Effects of Site Markers, Thermodynamics, Species Differences of Albumin-binding, and Influence of Albumin on Its Toxicity in MDCK Cells. Toxins 2018, 10, 353.

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