Binding of citreoviridin to human serum albumin: multispectroscopic and molecular docking.

Haifeng Hou,Baoxiu Jia,Xiaolan Qu,Xiaojun Yao,Baofa Jiang,Yueyue Kong,Yuqin Li

doi:10.1155/2015/162391

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.

Highlights

Citreoviridin (CIT, Figure 1), a toxic secondary metabolite produced by Penicillium citreoviride species [1], is a common contaminant of wide range of agriproducts and has a large range of toxic effects, and CIT has been associated with human health risks [2, 3]
The interaction of CIT with Human serum albumin (HSA) is investigated by optical spectroscopy technique and molecular modeling
It is found that the hydrophobic interactions and hydrogen bond forces play a major role in the binding of CIT with HSA

Summary

Introduction

Citreoviridin (CIT, Figure 1), a toxic secondary metabolite produced by Penicillium citreoviride species [1], is a common contaminant of wide range of agriproducts and has a large range of toxic effects, and CIT has been associated with human health risks [2, 3]. It is capable of binding to a wide variety of endogenous and exogenous compounds, such as fatty acids, hormones, toxics, and drugs, performing as carrier and transporter [8]. Studies have been conducted on the binding of organic contaminants or toxins to HSA, for example, arazine, ochratoxin A, methyl parathion, arsenic, perfluorooctanoic acid, patulin, deoxynivalenol, and 2-mercaptobenzimidazole [10,11,12,13,14,15,16,17]

Methods

Results

Conclusion