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

Zelma Faisal,Eszter Fliszár-Nyúl,Virág Vörös,Tamás Kőszegi,Ferenc Zsila,Sándor Kunsági-Máté,Rita Csepregi,Beáta Lemli,Miklós Poór

doi:10.3390/toxins12060392

Abstract

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.

Highlights

Mycotoxins are secondary fungal metabolites, which commonly contaminate food and feed, causing different toxic effects in animals and humans [1]
Since the inner filter effect of ochratoxins was negligible (the corrections were performed based on Equation (1)), these observations suggest the formation of mycotoxin–Human serum albumin (HSA) complexes
It is reasonable to conclude that the high-affinity binding site of ochratoxin B (OTB) and ochratoxin C (OTC) is located at Sudlow’s site I, similar to the parent mycotoxin ochratoxin A [30,31]

Summary

Introduction

Mycotoxins are secondary fungal metabolites, which commonly contaminate food and feed, causing different toxic effects in animals and humans [1]. Ochratoxins are produced by Aspergillus and Toxins 2020, 12, 392; doi:10.3390/toxins12060392 www.mdpi.com/journal/toxins. Toxins 2020, 12, x FOR PEER REVIEW. These nephrotoxic agents appear as contaminants in grains, cereal-based commodities, fruits, spices, and beverages (e.g., wine, beer, milk, and coffee) [3,4]. Other methodologies are required to obtain ochratoxin C (OTC), respectively—seem to be important (Figure 1). OTC is a toxic well-established conclusions, and extensive in vitro experiments as well as animal studies need to be to ochratoxin A, while OTB is less toxic [4]. Patulin (PAT; Figure 1) is produced by Aspergillus and performed for deeper understanding of mycotoxin–albumin interactions

Methods

Results

Conclusion