Simultaneous Detection of Tyrosine and Structure‐Specific Intrinsic Fluorescence in the Fibrillation of Alzheimer's Associated Peptides,ChemPhysChem

当前位置： X-MOL 学术 › ChemPhysChem › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

Simultaneous Detection of Tyrosine and Structure‐Specific Intrinsic Fluorescence in the Fibrillation of Alzheimer's Associated Peptides
ChemPhysChem ( IF 2.3 ) Pub Date : 2020-10-02 , DOI: 10.1002/cphc.202000587
Anurag Singh ₁ , Suparna Khatun ₁ , Amar Nath Gupta ₁

Affiliation

Understanding of the structural changes during their aggregation and interaction is a prerequisite for establishing the precise clinical relevance of human islet amyloid polypeptide (hIAPP) (involved in Type‐II Diabetes Mellitus) in the treatment of Alzheimer's disease stemmed from beta‐amyloid (Aβ). Herein, we show that the steady‐state emission spectra obtained from photoluminescence (PL) simultaneously capture both the tyrosine derivative (tyrosinate) and the structure‐specific intrinsic fluorescence during the aggregation of Aβ and hIAPP. We observe multiple peaks in the emission spectra which exist for structure‐specific intrinsic fluorescence, and use the second derivative UV‐Vis spectra and the shift in the tyrosine peak as a quantitative measure of the dissimilitude in the electronic states and the fibril growth. We further applied these techniques to detect the static electric field (0, 40, 120, 200 V/cm) induced promotion and inhibition of fibrillation in Aβ, hIAPP and their electric field dependent role in the fibrillation of Aβ : hIAPP(1 : 1). The results were corroborated by field‐emission scanning electron microscopy (FESEM), and the determinations of secondary structures by Fourier transform infrared spectroscopy (FTIR). The results indicate that the emission spectrum can be used as a sensor to detect the presence of fibrils; hence for screening potential inhibitors of amyloid fibrillation.

中文翻译：

同时检测阿尔茨海默氏症相关肽原纤化中的酪氨酸和特定结构的固有荧光。

了解其聚集和相互作用过程中的结构变化是确定人类胰岛淀粉样多肽（hIAPP）（涉及II型糖尿病）与因β-淀粉样蛋白（Aβ）引起的阿尔茨海默氏病的确切临床相关性的先决条件。本文中，我们显示了从光致发光（PL）获得的稳态发射光谱同时捕获了Aβ和hIAPP聚集期间的酪氨酸衍生物（酪氨酸盐）和结构特异性固有荧光。我们观察到发射光谱中存在多个结构特定的固有荧光峰，并使用二阶导数UV-Vis光谱和酪氨酸峰的位移作为电子状态和原纤维生长不相似性的定量度量。我们进一步应用了这些技术来检测静电场（0、40、120、200 V / cm）诱导和抑制Aβ，hIAPP的原纤维形成及其在Aβ：hIAPP（1：1的原纤维形成）中的电场依赖性作用）。场发射扫描电子显微镜（FESEM）证实了该结果，傅立叶变换红外光谱（FTIR）确定了二级结构。结果表明，发射光谱可以用作检测原纤维存在的传感器。因此用于筛选潜在的淀粉样蛋白原纤化抑制剂。场发射扫描电子显微镜（FESEM）证实了该结果，傅立叶变换红外光谱（FTIR）确定了二级结构。结果表明，发射光谱可以用作检测原纤维存在的传感器。因此用于筛选潜在的淀粉样蛋白原纤化抑制剂。场发射扫描电子显微镜（FESEM）证实了该结果，傅立叶变换红外光谱（FTIR）确定了二级结构。结果表明，发射光谱可以用作检测原纤维存在的传感器。因此用于筛选潜在的淀粉样蛋白原纤化抑制剂。

更新日期：2020-12-02

点击分享查看原文

点击收藏

阅读更多本刊最新论文本刊介绍/投稿指南11