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Toxins 2015, 7(12), 5155-5166; doi:10.3390/toxins7124871

Interaction of Citrinin with Human Serum Albumin

1
Department of Pharmacology and Pharmacotherapy, Toxicology Section, University of Pécs, Szigeti út 12, Pécs H-7624, Hungary
2
Department of General and Physical Chemistry, University of Pécs, Ifjúság útja 6, Pécs H-7624, Hungary
3
János Szentágothai Research Center, Ifjúság útja 20, Pécs H-7624, Hungary
4
Department of Biochemistry, Eötvös Loránd University, Pázmány sétány 1/C, Budapest 1117, Hungary
5
MTA-ELTE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Pázmány sétány 1/C, Budapest 1117, Hungary
6
Department of Laboratory Medicine, University of Pécs, Ifjúság útja 13, Pécs H-7624, Hungary
*
Author to whom correspondence should be addressed.
Academic Editor: HJ (Ine) van der Fels-Klerx
Received: 19 October 2015 / Revised: 22 November 2015 / Accepted: 25 November 2015 / Published: 1 December 2015
(This article belongs to the Section Mycotoxins)
View Full-Text   |   Download PDF [1492 KB, uploaded 1 December 2015]   |  

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. View Full-Text
Keywords: citrinin; human serum albumin; fluorescence spectroscopy; ultrafiltration; species differences citrinin; human serum albumin; fluorescence spectroscopy; ultrafiltration; species differences
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Poór, M.; Lemli, B.; Bálint, M.; Hetényi, C.; Sali, N.; Kőszegi, T.; Kunsági-Máté, S. Interaction of Citrinin with Human Serum Albumin. Toxins 2015, 7, 5155-5166.

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