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Study of Methylene Blue Interaction with Human Serum Albumin

机译:与人血清白蛋白的亚甲基蓝相互作用研究

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The thiosine dye methylene blue (MB) interaction with human serum albumin (HSA) has been studied. MB was revealed to stabilize the native structure of HSA, since the denaturation temperature of the complexes is shifted to higher values in relation to that of the pure protein. It was also revealed that the absorption spectra of the complexes do not change noticeably, while in the fluorescence spectra the maximal intensity of MB decreases with the albumin concentration enhancement. Analysis of the obtained data allows to conclude that the main binding mode of MB to HSA, providing the stabilization of the protein native structure, is the electrostatic mechanism.
机译:研究了与人血清白蛋白(HSA)的硫酸钠亚甲基蓝(MB)相互作用。 显示MB以稳定HSA的天然结构,因为复合物的变性温度被移位为与纯蛋白质的更高值。 还揭示了复合物的吸收光谱在荧光光谱中不会显着变化,而MB的最大强度随着白蛋白浓度的增强而降低。 所获得的数据的分析允许得出结论,MB对HSA的主要结合模式,提供蛋白质天然结构的稳定,是静电机制。

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