Interaction between quinoline yellow and human serum albumin: Spectroscopic, chemometrics and molecular docking studies
Interaction between quinoline yellow and human serum albumin: Spectroscopic, chemometrics and molecular docking studies
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喹啉黄与人血清白蛋白之间的相互作用：光谱、化学计量学和分子对接研究
DOI：
10.1002/jsfa.9144
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发表时间：
2019
影响因子：
4.1
通讯作者：
Guowen Zhang
中科院分区：
文献类型：
--
作者：
Rui Wang;Xing Hu;Junhui Pan;Deming Gong;Guowen Zhang
背景喹啉黄(QY)是一种广泛应用于食品工业的合成着色剂，因其对人体健康的潜在危害而引起广泛关注。本工作采用多种光谱方法、化学计量学算法和分子模拟方法研究了QY与人血清白蛋白(HSA)的相互作用。结果通过多元曲线分辨交替最小二乘法分析扩展的UV-可见光吸收数据矩阵，得到了QY、HSA和QY-HSA络合物的浓度分布和纯光谱，证实了QY-HSA的相互作用过程。QY通过形成中等亲和力稳定的QY-HSA络合物来猝灭HSA的荧光。疏水作用力和氢键在QY与人血清白蛋白的结合中起主要作用。位点特异性标记诱导的位移结果表明，QY与HSA的IIA亚域结合。分子对接结果证实了这一点。HSA表面疏水性和游离巯基含量的降低表明，QY导致HSA中的肽链收缩，隐藏了蛋白质的疏水斑块。通过紫外-可见吸收光谱、圆二色谱和三维荧光光谱的分析发现，QY引起了荧光团周围的微环境扰动和HSA二级结构的变化。结论本工作表明QY与HSA结合，影响其结构和功能性质，为深入了解QY的结合机理和对生物过程的毒性提供了新的见解。2018年中国化学工业学会
BACKGROUNDQuinoline yellow (QY), a synthetic colourant widely used in the food industry, has caused extensive concerns because of its potentially harmful effects on human health. In the present work, the interactions between QY and human serum albumin (HSA) were characterized by multiple spectroscopic methods, a chemometric algorithm, and molecular modelling studies.RESULTSThe concentration profiles and pure spectra obtained for the components (QY, HSA and QY–HSA complex) from analyses of the expanded UV‐visible absorption data matrices by multivariate curve resolution alternating least squares confirmed the QY–HSA interaction process. QY quenched the fluorescence of HSA through formation of a QY–HSA complex that was stabilized by moderate affinity. Hydrophobic forces and hydrogen bonding play major roles in the binding of QY to HSA. Site‐specific marker‐induced displacement results suggest that QY binds to subdomain IIA of HSA. This was corroborated by the molecular docking results. Decreases in HSA surface hydrophobicity and free sulfhydryl group content indicate that QY causes a contraction of the peptide strand in HSA, hiding the hydrophobic patches of the protein. Analyses by UV‐visible absorption, circular dichroism, and three‐dimensional fluorescence spectroscopy found that QY causes microenvironmental perturbations around the fluorophores and secondary structure changes in HSA.CONCLUSIONThis work shows that QY binds to HSA, affecting its structural and functional properties, and provides new insights into the binding mechanism and a comprehensive understanding of the toxicity of QY to biological processes. © 2018 Society of Chemical Industry