Insulin amyloid fibrillation studied by terahertz spectroscopy and other biophysical methods
Insulin amyloid fibrillation studied by terahertz spectroscopy and other biophysical methods
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通过太赫兹光谱和其他生物物理方法研究胰岛素淀粉样纤维颤动
DOI：
10.1016/j.bbrc.2009.11.153
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发表时间：
2010-01-01
影响因子：
3.1
通讯作者：
He, Zhimin
中科院分区：
文献类型：
--
作者：
Liu, Rui;He, Mingxia;He, Zhimin
淀粉样蛋白的组装和纤颤被认为在各种人类疾病的病因学中起着关键作用，包括阿尔茨海默病、帕金森病、亨廷顿舞蹈症和II型糖尿病。洞察构象变化和形成过程中淀粉样蛋白颤动是必不可少的临床诊断和药物发现。研究二级、三级、四级结构的变化。在60℃条件下，将牛胰岛素在20%醋酸中孵育，并采用圆二色性（CD）、硫黄素T荧光（ThT）、动态光散射（DLS）、电子显微镜和太赫兹（THz）吸收光谱等多种生物物理技术对其多层结构进行研究。实验数据表明，从26 h开始，α -螺旋转变为β -薄片，随后是胰岛素的聚集，如ThT结合所示，在41 h时发生过渡中点，约71 h后形成大量成熟聚集体。太赫兹是一种快速且无创的技术。我们首先应用太赫兹光谱对淀粉样蛋白颤动进行了研究。在0.2-2.0太赫兹的太赫兹频率范围内，太赫兹光谱的吸光度和折射率都有明显的增加。因此，太赫兹有望提供一种研究淀粉样纤维性颤动的新方法。(C) 2009爱思唯尔公司版权所有。
Assembly and fibrillation of amyloid proteins are believed to play a key role in the etiology of various human diseases, including Alzheimer's, Parkinson's, Huntington's and type II diabetes. Insights into conformational changes and formation processes during amyloid fibrillation are essential for the clinical diagnosis and drug discovery. To study the changes in secondary, tertiary, quaternary Structures. and the alteration in the collective vibrational mode density of states during the amyloid fibrillation, bovine insulin in 20% acetic acid was incubated at 60 degrees C, and its multi-level structures were followed by Various biophysical techniques, including circular dichroism (CD), thioflavin T fluorescence (ThT), dynamic light scattering (DLS), electron microscopy, and terahertz (THz) absorption spectroscopy. The experimental data demonstrated a transformation of alpha-helix into beta-sheet starting at 26 It This was followed by the aggregation of Insulin, as shown by ThT binding, with a transition midpoint at 41 h, and by the bulk formation of mature aggregates after about 71 h. THz is a quick and non-invasive technique, which has the advantage of allowing the study of the conformational state of biomolecules and tissues We first applied THz spectroscopy to study the amyloid fibrillation At the terahertz frequency range of 0.2-2.0 THz, there was an apparent increase in both the absorbance and refractive index in THz spectra. Thus, THz is expected to provide a new way of looking into amyloid fibrillation. (C) 2009 Elsevier Inc. All rights reserved.