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ARS Home » Midwest Area » Peoria, Illinois » National Center for Agricultural Utilization Research » Mycotoxin Prevention and Applied Microbiology Research » Research » Publications at this Location » Publication #313322
Title: Interaction of zearalenone with bovine serum albumin as determined by fluorescence quenching

Author
item MA, LIANG - Southwest University
item ZHANG, YUHAO - Southwest University
item Maragos, Chris

Submitted to: Mycotoxin Research
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 10/26/2017
Publication Date: 11/13/2017
Citation: Ma, L., Zhang, Y., Maragos, C.M. 2017. Interaction of zearalenone with bovine serum albumin as determined by fluorescence quenching. Mycotoxin Research. 34(1):39-48.

Interpretive Summary: Zearalenone (ZEA) is a secondary metabolite produced by certain fungi that commonly infest important cereal crops, including corn and wheat. ZEA exhibits a wide range of toxic effects but is primarily known for its activity as a potent estrogen. Binding of ZEA to proteins in the blood, such as albumin, is one factor that could influence the distribution and elimination of ZEA. To provide insights into how ZEA might be distributed within the body following exposure, we investigated the interaction between ZEA and bovine serum albumin (BSA). Results indicated that ZEA does indeed bind to BSA, and does so with strong affinity, suggesting that serum albumins are likely involved in the distribution of this mycotoxin throughout the body following exposure. This information helps to explain how ZEA exposure is related toxicity and will be helpful in efforts to mitigate the effects of this toxin.

Technical Abstract: The major aim of this study was to examine the binding of zearalenone (ZEN) to bovine serum albumin (BSA) by measuring the quenching of the intrinsic fluorescence of the protein under aqueous conditions. The results suggest that ZEN has a strong ability to quench the intrinsic fluorescence of BSA through a static mechanism. The hydrophobicity of the microenvironment around the tyrosine (Tyr) residues in BSA was increased in the presence of ZEN. The quenching constants, ratio of protein with ZEN, and thermodynamic parameters were determined. The collaborative action of hydrophobic and electrostatic interactions was involved in the binding process and the formation of the complex was mainly enthalpy-driven. The average binding distance between ZEN and BSA was calculated to be 2.20 nm. This is much closer in magnitude than the distance reported for the binding of most toxins to HSA and most pharmaceuticals to BSA, indicating a strong affinity.