Interaction of Citrinin with Human Serum Albumin

Poór, Miklós; Lemli, Beáta; Bálint, Mónika; Hetényi, Csaba; Sali, Nikolett; Kőszegi, Tamás; Kunsági-Máté, Sándor

doi:10.3390/toxins7124871

Open AccessArticle

Interaction of Citrinin with Human Serum Albumin

by

Miklós Poór

^1,*,

Beáta Lemli

^2,3,

Mónika Bálint

⁴,

Csaba Hetényi

⁵,

Nikolett Sali

^3,6,

Tamás Kőszegi

^3,6

and

Sándor Kunsági-Máté

^2,3

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.

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

Submission received: 19 October 2015 / Revised: 22 November 2015 / Accepted: 25 November 2015 / Published: 1 December 2015

(This article belongs to the Section Mycotoxins)

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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.

Keywords: citrinin; human serum albumin; fluorescence spectroscopy; ultrafiltration; species differences

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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. https://doi.org/10.3390/toxins7124871

AMA 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(12):5155-5166. https://doi.org/10.3390/toxins7124871

Chicago/Turabian Style

Poór, Miklós, Beáta Lemli, Mónika Bálint, Csaba Hetényi, Nikolett Sali, Tamás Kőszegi, and Sándor Kunsági-Máté. 2015. "Interaction of Citrinin with Human Serum Albumin" Toxins 7, no. 12: 5155-5166. https://doi.org/10.3390/toxins7124871

APA Style

Poór, M., Lemli, B., Bálint, M., Hetényi, C., Sali, N., Kőszegi, T., & Kunsági-Máté, S. (2015). Interaction of Citrinin with Human Serum Albumin. Toxins, 7(12), 5155-5166. https://doi.org/10.3390/toxins7124871

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Interaction of Citrinin with Human Serum Albumin

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