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BioMed Research International
Volume 2015, Article ID 162391, 8 pages
http://dx.doi.org/10.1155/2015/162391
Research Article

Binding of Citreoviridin to Human Serum Albumin: Multispectroscopic and Molecular Docking

1School of Public Health, Shandong University, Jinan 250012, China
2School of Public Health, Taishan Medical University, Taian 271016, China
3School of Pharmacy, Taishan Medical University, Taian 271016, China
4School of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou 271000, China

Received 17 February 2015; Revised 25 March 2015; Accepted 27 March 2015

Academic Editor: Maxim P. Evstigneev

Copyright © 2015 Haifeng Hou et al. 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.

Abstract

Citreoviridin (CIT), a mycotoxin produced by Penicillium citreonigrum, is a common contaminant of wide range of agriproducts and detrimental to human and animal health. In this study, the interaction of CIT with human serum albumin (HSA) is researched by steady-state fluorescence, ultraviolet-visible (UV-Vis) absorption, circular dichroism (CD) methods, and molecular modeling. The association constants, binding site numbers, and corresponding thermodynamic parameters are used to investigate the quenching mechanism. The alternations of HSA secondary structure in the presence of CIT are demonstrated with UV-Vis, synchronous fluorescence, and CD spectra. The molecular modeling results reveal that CIT can bind with hydrophobic pocket of HSA with hydrophobic and hydrogen bond force. Moreover, an apparent distance of 3.25 nm between Trp214 and CIT is obtained via fluorescence resonance energy transfer method.