Yuhan Huang, Gary S Cooney, David Talaga, Renaud A L Vallée, Rossana Quinzi, Laurent Bouffier, Sophie Lecomte, Sébastien Bonhommeau
{"title":"利用全内反射尖端增强拉曼光谱对水中淀粉样蛋白纤维进行纳米级化学成像。","authors":"Yuhan Huang, Gary S Cooney, David Talaga, Renaud A L Vallée, Rossana Quinzi, Laurent Bouffier, Sophie Lecomte, Sébastien Bonhommeau","doi":"10.1021/acs.jpclett.4c02309","DOIUrl":null,"url":null,"abstract":"<p><p>Total-internal-reflection tip-enhanced Raman spectroscopy (TIR-TERS) imaging of amyloid-β (Aβ<sub>1-42</sub>-L34T) fibrils is performed with nanoscale spatial resolution in water, using TERS tips fabricated by bipolar electrodeposition. Ideal experimental parameters are corroborated by both theoretical simulations and TIR-TERS measurements. TIR-TERS imaging reveals the predominant parallel β-sheet secondary structure of Aβ<sub>1-42</sub>-L34T fibrils as well as the nanoscale spatial distribution of tyrosine, histidine, and phenylalanine aromatic amino acids. Their proportion in TERS spectra can be qualitatively explained by the combined effect of their localization in the Aβ<sub>1-42</sub>-L34T fibril structure and their molecular orientation with respect to the excitation laser light polarization. Conclusions drawn from the TERS experiments in water corroborate and significantly enrich our previous study in ambient air, thus confirming that hydration has only a marginal impact on the structure of such amyloid fibrils. This first TIR-TERS study in liquid opens fascinating perspectives for future applications in biology.</p>","PeriodicalId":62,"journal":{"name":"The Journal of Physical Chemistry Letters","volume":null,"pages":null},"PeriodicalIF":4.8000,"publicationDate":"2024-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Nanoscale Chemical Imaging of Amyloid Fibrils in Water Using Total-Internal-Reflection Tip-Enhanced Raman Spectroscopy.\",\"authors\":\"Yuhan Huang, Gary S Cooney, David Talaga, Renaud A L Vallée, Rossana Quinzi, Laurent Bouffier, Sophie Lecomte, Sébastien Bonhommeau\",\"doi\":\"10.1021/acs.jpclett.4c02309\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Total-internal-reflection tip-enhanced Raman spectroscopy (TIR-TERS) imaging of amyloid-β (Aβ<sub>1-42</sub>-L34T) fibrils is performed with nanoscale spatial resolution in water, using TERS tips fabricated by bipolar electrodeposition. Ideal experimental parameters are corroborated by both theoretical simulations and TIR-TERS measurements. TIR-TERS imaging reveals the predominant parallel β-sheet secondary structure of Aβ<sub>1-42</sub>-L34T fibrils as well as the nanoscale spatial distribution of tyrosine, histidine, and phenylalanine aromatic amino acids. Their proportion in TERS spectra can be qualitatively explained by the combined effect of their localization in the Aβ<sub>1-42</sub>-L34T fibril structure and their molecular orientation with respect to the excitation laser light polarization. Conclusions drawn from the TERS experiments in water corroborate and significantly enrich our previous study in ambient air, thus confirming that hydration has only a marginal impact on the structure of such amyloid fibrils. This first TIR-TERS study in liquid opens fascinating perspectives for future applications in biology.</p>\",\"PeriodicalId\":62,\"journal\":{\"name\":\"The Journal of Physical Chemistry Letters\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":4.8000,\"publicationDate\":\"2024-10-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The Journal of Physical Chemistry Letters\",\"FirstCategoryId\":\"1\",\"ListUrlMain\":\"https://doi.org/10.1021/acs.jpclett.4c02309\",\"RegionNum\":2,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/10/1 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Journal of Physical Chemistry Letters","FirstCategoryId":"1","ListUrlMain":"https://doi.org/10.1021/acs.jpclett.4c02309","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/10/1 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
引用次数: 0
摘要
利用双极电沉积法制造的 TERS 头，在水中对淀粉样蛋白-β（Aβ1-42-L34T）纤维进行了具有纳米级空间分辨率的全内反射尖端增强拉曼光谱（TIR-TERS）成像。理想的实验参数得到了理论模拟和 TIR-TERS 测量的证实。TIR-TERS 成像揭示了 Aβ1-42-L34T 纤维的主要平行 β 片二级结构，以及酪氨酸、组氨酸和苯丙氨酸芳香族氨基酸的纳米级空间分布。它们在 TERS 光谱中的比例可以通过它们在 Aβ1-42-L34T 纤维结构中的定位及其相对于激发激光偏振的分子取向的综合效应得到定性解释。在水中进行的 TERS 实验得出的结论证实并极大地丰富了我们之前在环境空气中进行的研究，从而证实了水合作用对这种淀粉样蛋白纤维结构的影响微乎其微。这项首次在液体中进行的 TIR-TERS 研究为未来在生物学中的应用开辟了迷人的前景。
Nanoscale Chemical Imaging of Amyloid Fibrils in Water Using Total-Internal-Reflection Tip-Enhanced Raman Spectroscopy.
Total-internal-reflection tip-enhanced Raman spectroscopy (TIR-TERS) imaging of amyloid-β (Aβ1-42-L34T) fibrils is performed with nanoscale spatial resolution in water, using TERS tips fabricated by bipolar electrodeposition. Ideal experimental parameters are corroborated by both theoretical simulations and TIR-TERS measurements. TIR-TERS imaging reveals the predominant parallel β-sheet secondary structure of Aβ1-42-L34T fibrils as well as the nanoscale spatial distribution of tyrosine, histidine, and phenylalanine aromatic amino acids. Their proportion in TERS spectra can be qualitatively explained by the combined effect of their localization in the Aβ1-42-L34T fibril structure and their molecular orientation with respect to the excitation laser light polarization. Conclusions drawn from the TERS experiments in water corroborate and significantly enrich our previous study in ambient air, thus confirming that hydration has only a marginal impact on the structure of such amyloid fibrils. This first TIR-TERS study in liquid opens fascinating perspectives for future applications in biology.
期刊介绍：
The Journal of Physical Chemistry (JPC) Letters is devoted to reporting new and original experimental and theoretical basic research of interest to physical chemists, biophysical chemists, chemical physicists, physicists, material scientists, and engineers. An important criterion for acceptance is that the paper reports a significant scientific advance and/or physical insight such that rapid publication is essential. Two issues of JPC Letters are published each month.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
