Spatially resolved spectroscopic differentiation of hydrophilic and hydrophobic domains on individual insulin amyloid fibrils.
Spatially resolved spectroscopic differentiation of hydrophilic and hydrophobic domains on individual insulin amyloid fibrils.
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DOI：
10.1038/srep33575
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发表时间：
2016-09-21
影响因子：
4.6
通讯作者：
Deckert V
中科院分区：
文献类型：
--
作者：
Deckert-Gaudig T;Kurouski D;Hedegaard MA;Singh P;Lednev IK;Deckert V
被称为淀粉样蛋白原纤维的不溶性富含β-片层的蛋白质结构的形成与许多神经退行性疾病相关，例如阿尔茨海默病和帕金森病。纤维表面的分子结构的详细理解是感兴趣的，因为它是与体内生理环境的第一次接触，并且在生物活性和相关毒性中起决定性作用。最近的研究表明，尖端增强拉曼散射（TERS）的固有灵敏度和特异性，使这项技术成为一个引人注目的方法，在单颗粒水平的原纤维表面分析。在这里，TERS的再现性被证明，表明其检测分子变异的相关性。因此，个别原纤维系统地研究在纳米空间分辨率。光谱参数通过带拟合获得，特别是侧重于通过酰胺III带和表面上的疏水和亲水域的分化的二级结构的识别。此外，多变量数据分析，特别是N-FINDR程序，用于生成结构特异性图谱。TERS在原纤维表面上定位特定结构域的能力显示出开发新的原纤维解剖策略的希望，并且当感兴趣的是纳米水平的结构变化时，可以通常应用于任何（生物）化学表面。
The formation of insoluble β-sheet-rich protein structures known as amyloid fibrils is associated with numerous neurodegenerative diseases, such as Alzheimer’s and Parkinson’s disease. A detailed understanding of the molecular structure of the fibril surface is of interest as the first contact with the physiological environment in vivo and plays a decisive role in biological activity and associated toxicity. Recent studies reveal that the inherent sensitivity and specificity of tip-enhanced Raman scattering (TERS) renders this technique a compelling method for fibril surface analysis at the single-particle level. Here, the reproducibility of TERS is demonstrated, indicating its relevance for detecting molecular variations. Consequently, individual fibrils are systematically investigated at nanometer spatial resolution. Spectral parameters were obtained by band-fitting, particularly focusing on the identification of the secondary structure via the amide III band and the differentiation of hydrophobic and hydrophilic domains on the surface. In addition multivariate data analysis, specifically the N-FINDR procedure, was employed to generate structure-specific maps. The ability of TERS to localize specific structural domains on fibril surfaces shows promise to the development of new fibril dissection strategies and can be generally applied to any (bio)chemical surface when structural variations at the nanometer level are of interest.
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