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Interaction of toxic azo dyes with heme protein: Biophysical insights into the binding aspect of the food additive amaranth with human hemoglobin

机译:有毒的偶氮染料与血红素蛋白的相互作用:食品添加剂mar菜红与人血红蛋白结合方面的生物物理见解

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A biophysical study on the interaction of the food colorant amaranth with hemoglobin was undertaken. Spectrophotometric and spectrofluorimetric studies proposed for an intimate binding interaction between the dye and the protein. The dye quenched the fluorescence of the protein remarkably and the mechanism of quenching was found to be static in nature. Synchronous fluorescence studies suggested that the polarity around the tryptophan residues was altered in the presence of amaranth whereas the polarity around tyrosine residues remained largely unaltered. 3D fluorescence, FTIR and circular dichroism results suggested that the binding reaction caused conformational changes in hemoglobin. The negative far-UV CD bands exhibited a significantly large decrease in magnitude in the presence of amaranth. From calorimetry studies it was established that the binding was driven by a large positive entropic contribution and a small but favorable enthalpy change. (C) 2015 Elsevier B.V. All rights reserved.
机译:进行了食用色素a菜与血红蛋白相互作用的生物物理研究。分光光度法和荧光分光光度法研究提出了染料与蛋白质之间紧密结合的相互作用。该染料显着地淬灭了蛋白质的荧光,并且发现淬灭的机制本质上是静态的。同步荧光研究表明,在a菜红的存在下,色氨酸残基周围的极性发生了变化,而酪氨酸残基周围的极性则基本保持不变。 3D荧光,FTIR和圆二色性结果表明,结合反应引起血红蛋白的构象变化。在a菜存在的情况下,远紫外线CD负谱带的幅度明显降低。从量热法研究中可以确定,结合是由较大的正熵贡献和较小但有利的焓变驱动的。 (C)2015 Elsevier B.V.保留所有权利。

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