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Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

机译:各种变性条件下人血清白蛋白的二次结构变化的系统性FTIR光谱研究

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摘要

Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.
机译:人血清白蛋白(HSA)是血浆中最丰富的蛋白质。 HSA涉及荷尔蒙,脂肪酸和其他一些化合物的运输,维持血液pH,渗透压等许多功能。虽然该蛋白质进行了很好的研究,但对不同变性因子的构象变化的数据是零碎的,有时是矛盾的。对于FTIR光谱数据解释尤其如此。这里,系统地研究了各种变性剂在水溶液中使用FTIR光谱法在HSA结构状态下的影响。我们的数据表明,第二衍生物解卷积方法提供了所获得的IR光谱的最一致的解释。根据酸,碱性和热变性期间的变性剂的浓度研究了HSA的二次结构变化。通常,在不同条件下的HSA的变性伴随着α-螺旋构象的降低和随机线圈构象的增加和分子间β-股。同时,还观察到根据变性剂的类型的构象变化的一些变化。 β-结构构象的增加表明,HSA可以在变性时形成淀粉样蛋白样聚集体。

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