The secondary structure of pressure- and temperature-induced aggregates of equine serum albumin studied by FT-IR spectroscopy.
The secondary structure of pressure- and temperature-induced aggregates of equine serum albumin studied by FT-IR spectroscopy.
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DOI：
10.1016/j.bbapap.2006.06.006
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发表时间：
2006-08
期刊：
影响因子：
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通讯作者：
A. Okuno;Minoru Katō;Y. Taniguchi
中科院分区：
文献类型：
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作者：
A. Okuno;Minoru Katō;Y. Taniguchi
蛋白质聚集体分为淀粉样纤维和无定形聚集体。淀粉样原纤维由三维有序结构组成，并与硫磺素T和刚果红染料结合。具有无序结构的无定形聚集体不与这些染料结合。我们研究了压力和热诱导的聚集体的马血清白蛋白（ESA）的二级结构的观点，使用FT-IR光谱。我们显示了二级结构之间的差异热和压力诱导的ESA聚集体。ESA的热诱导不可逆聚集体由分子间β-折叠结构组成，不与硫黄T和刚果红结合而形成无定形聚集体。另一方面，压力诱导的可逆聚集体由无规结构组成，也是无定形形式。从ESA在本地和还原条件下的二硫键的压力效应的比较，我们证明，由二硫键的结构灵活性的限制是一个重要的因素，压力诱导的聚集的可逆性。
The protein aggregation is divided into amyloid fibrils and amorphous aggregates. Amyloid fibrils are composed of the 3-dimensional ordered structure and are bound to thioflavin T and Congo red dyes. The amorphous aggregates with the disordered structure do not bind to these dyes. We have investigated the pressure- and heat-induced aggregates of equine serum albumin (ESA) from the secondary structural viewpoint using FT-IR spectroscopy. We show the secondary structural differences between heat- and pressure-induced aggregates of ESA. The heat-induced irreversible aggregates of ESA are composed of the intermolecular β-sheet structure without binding thioflavie T and Congo red to be amorphous form. On the other hand, the pressure-induced reversible aggregates are composed of the random structure to be also amorphous form. From the comparison of pressure effects on ESA in native and reducing conditions of disulfide bridges, we demonstrate that the restriction of structural flexibility by disulfide bridges is an important factor for the reversibility of the pressure-induced aggregation.