Pressure effects on the structure, kinetic, and thermodynamic properties of heat-induced aggregation of protein studied by FT-IR spectroscopy
Pressure effects on the structure, kinetic, and thermodynamic properties of heat-induced aggregation of protein studied by FT-IR spectroscopy
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通过 FT-IR 光谱研究压力对热诱导蛋白质聚集的结构、动力学和热力学性质的影响
DOI：
10.1088/1742-6596/215/1/012156
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发表时间：
2010
期刊：
影响因子：
--
通讯作者：
M. Kato
中科院分区：
文献类型：
--
作者：
Y. Taniguchi;A. Okuno;M. Kato
压力可以抑制热诱导的聚集体并使热诱导的聚集体解离。采用傅立叶变换红外光谱（FT-IR）研究了马血清白蛋白（ESA）热诱导聚集的压力抑制效应和压力解离效应。结果表明，在热诱导聚集过程中，α-螺旋结构首先通过溶胀结构坍塌，然后通过部分未折叠结构重排为分子间β-折叠。我们测定了热诱导聚集体的活化体积（ΔV# = +93 ml/mol）以及天然状态和热诱导聚集体之间的偏摩尔体积差（ΔV=+32 ml/mol）。这种正偏摩尔体积差表明热诱导聚集体具有比天然结构更大的内部空隙。此外，正体积变化意味着在高压下分子间β-折叠的形成是不利的。
Pressure can retrain the heat-induced aggregation and dissociate the heat-induced aggregates. We observed the aggregation-preventing pressure effect and the aggregates-dissociating pressure effect to characterize the heat-induced aggregation of equine serum albumin (ESA) by FT-IR spectroscopy. The results suggest the α-helical structure collapses at the beginning of heat-induced aggregation through the swollen structure, and then the rearrangement of structure to the intermolecular β-sheet takes place through partially unfolded structure. We determined the activation volume for the heat-induced aggregation (ΔV# = +93 ml/mol) and the partial molar volume difference between native state and heat-induced aggregates (ΔV=+32 ml/mol). This positive partial molar volume difference suggests that the heat-induced aggregates have larger internal voids than the native structure. Moreover, the positive volume change implies that the formation of the intermolecular β-sheet is unfavorable under high pressure.