College of Food Science, Southwest University, No. 2 Tiansheng Road, Beibei District of ChongQing, 400716, China.
Mycotoxin Prevention and Applied Microbiology Research Unit, National Center for Agricultural Utilization Research, ARS, USDA, 1815 N, University Street, Peoria, IL, 61604, USA.
Mycotoxin Res. 2018 Mar;34(1):39-48. doi: 10.1007/s12550-017-0297-7. Epub 2017 Nov 13.
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.
本研究的主要目的是通过测量水溶液中蛋白质内源荧光的猝灭来研究玉米赤霉烯酮（ZEN）与牛血清白蛋白（BSA）的结合。结果表明，ZEN 能够通过静态机制强烈猝灭 BSA 的内源荧光。在 ZEN 存在的情况下，BSA 中酪氨酸（Tyr）残基周围微环境的疏水性增加。测定了猝灭常数、与 ZEN 结合的蛋白质比例和热力学参数。结合过程涉及疏水相互作用和静电相互作用的协同作用，复合物的形成主要是由焓驱动的。计算得出 ZEN 与 BSA 之间的平均结合距离为 2.20nm。这一数值与大多数毒素与 HSA 结合以及大多数药物与 BSA 结合的距离相比，数值要小得多，表明两者之间具有很强的亲和力。
