Interaction of Citrinin with Human Serum Albumin
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 st...
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| Format: | Article |
| Language: | English |
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MDPI AG
2015-12-01
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| Series: | Toxins |
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| Online Access: | http://www.mdpi.com/2072-6651/7/12/4871 |
| _version_ | 1828393587373506560 |
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| author | Miklós Poór Beáta Lemli Mónika Bálint Csaba Hetényi Nikolett Sali Tamás Kőszegi Sándor Kunsági-Máté |
| author_facet | Miklós Poór Beáta Lemli Mónika Bálint Csaba Hetényi Nikolett Sali Tamás Kőszegi Sándor Kunsági-Máté |
| author_sort | Miklós Poór |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-10T07:41:26Z |
| format | Article |
| id | doaj.art-8ed4045399a646d1a9db288d94e59c24 |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-12-10T07:41:26Z |
| publishDate | 2015-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-8ed4045399a646d1a9db288d94e59c242022-12-22T01:57:18ZengMDPI AGToxins2072-66512015-12-017125155516610.3390/toxins7124871toxins7124871Interaction of Citrinin with Human Serum AlbuminMiklós Poór0Beáta Lemli1Mónika Bálint2Csaba Hetényi3Nikolett Sali4Tamás Kőszegi5Sándor Kunsági-Máté6Department of Pharmacology and Pharmacotherapy, Toxicology Section, University of Pécs, Szigeti út 12, Pécs H-7624, HungaryDepartment of General and Physical Chemistry, University of Pécs, Ifjúság útja 6, Pécs H-7624, HungaryDepartment of Biochemistry, Eötvös Loránd University, Pázmány sétány 1/C, Budapest 1117, HungaryMTA-ELTE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Pázmány sétány 1/C, Budapest 1117, HungaryJános Szentágothai Research Center, Ifjúság útja 20, Pécs H-7624, HungaryJános Szentágothai Research Center, Ifjúság útja 20, Pécs H-7624, HungaryDepartment of General and Physical Chemistry, University of Pécs, Ifjúság útja 6, Pécs H-7624, HungaryCitrinin (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.http://www.mdpi.com/2072-6651/7/12/4871citrininhuman serum albuminfluorescence spectroscopyultrafiltrationspecies differences |
| spellingShingle | Miklós Poór Beáta Lemli Mónika Bálint Csaba Hetényi Nikolett Sali Tamás Kőszegi Sándor Kunsági-Máté Interaction of Citrinin with Human Serum Albumin Toxins citrinin human serum albumin fluorescence spectroscopy ultrafiltration species differences |
| title | Interaction of Citrinin with Human Serum Albumin |
| title_full | Interaction of Citrinin with Human Serum Albumin |
| title_fullStr | Interaction of Citrinin with Human Serum Albumin |
| title_full_unstemmed | Interaction of Citrinin with Human Serum Albumin |
| title_short | Interaction of Citrinin with Human Serum Albumin |
| title_sort | interaction of citrinin with human serum albumin |
| topic | citrinin human serum albumin fluorescence spectroscopy ultrafiltration species differences |
| url | http://www.mdpi.com/2072-6651/7/12/4871 |
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