Abstract
Citrinin (CIT) is a mycotoxin produced by several Aspergillus, Penicillium, and Monascus species. CIT occurs worldwide in different foods and drinks and causes health problems for humans and animals. Human serum albumin (HSA) is the most abundant plasma protein in human circulation. Albumin forms stable complexes with many drugs and xenobiotics; therefore, HSA commonly plays important role in the pharmacokinetics or toxicokinetics of numerous compounds. However, the interaction of CIT with HSA is poorly characterized yet. In this study, the complex formation of CIT with HSA was investigated using fluorescence spectroscopy and ultrafiltration techniques. For the deeper understanding of the interaction, thermodynamic, and molecular modeling studies were performed as well. Our results suggest that CIT forms stable complex with HSA (logK ~ 5.3) and its primary binding site is located in subdomain IIA (Sudlow’s Site I). In vitro cell experiments also recommend that CIT-HSA interaction may have biological relevance. Finally, the complex formations of CIT with bovine, porcine, and rat serum albumin were investigated, in order to test the potential species differences of CIT-albumin interactions.
Highlights
Mycotoxins are toxic secondary metabolites produced naturally by filamentous fungi
Our results clearly demonstrate that CIT forms a stable the stability of CIT‐Human serum albumin (HSA) complex, as well as to identify the primary binding site of CIT on complex with albumin suggesting theunderstanding potential inofvivo relevance of the interaction, which one should the HSA molecule
The very similar P values in presence of CIT and warfarin recommend that the displacing abilities of CIT and warfarin and freedom of free ochratoxin A (OTA) is much higher compared to its albumin-bound form, the decrease of fluorescence polarization values suggests the molecular displacement of OTA from HSA [25,26]
Summary
Mycotoxins are toxic secondary metabolites produced naturally by filamentous fungi. Due to their wide occurrence, mycotoxin contamination of various foods, drinks, and animal feed is unavoidable, causing serious health problems for humans and animals [1]. Very relevant interactions of HSA with mycotoxins occur, e.g., in the case of ochratoxin investigations highlighted that both. Was investigated using and pseudo‐enzymatic activities addition, one of the most important functions of HSA is the binding (and in this route the transport) of numerous endogenous molecules, drugs, and xenobiotics; fluorescence spectroscopy, ultrafiltration, and molecular docking studies. Our main goals were to HSA can a major complex, role in their as pharmacokinetics/toxicokinetics in many cases [13,14].site of CIT determinetherefore, the stability of play. Our results clearly demonstrate that CIT forms a stable the stability of CIT‐HSA complex, as well as to identify the primary binding site of CIT on complex with albumin suggesting theunderstanding potential inofvivo relevance of the interaction, which one should the HSA molecule. Interactions of with bovine, porcine, and rat serum albumin were investigated to explore the possible
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