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Electrochemical quantification of the Alzheimer’s disease amyloid-β (1–40) using amyloid-β fibrillization promoting peptide

机译:淀粉样β-原纤维化促进肽对阿尔茨海默氏病淀粉样-β(1-4)的电化学定量

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Abstract Amyloid-β peptide (Aβ) is believed to be an important biomarker for the early diagnosis of Alzheimer’s disease. Therefore, practical and reliable methods to assay Aβ levels have been coveted. In this study, a rapid, sensitive, and selective electrochemical method for Aβ(1–40) detection using Cu2+ redox cycling on peptide-modified gold electrodes was developed. A 19-residue peptide that can promote Aβ fibrillization (AFPP) was immobilized onto a gold electrode. After incubating an Aβ solution with the modified electrode for 1 h, a Cu2+ solution was added and cyclic voltammetry measurements were conducted. The voltammetric response was found to be proportional to the Aβ(1–40) concentration in the 0.1–5 μM range, and a detection limit of 18 nM was achieved. Washing with sodium hydroxide and ethylenediaminetetraacetate solutions easily reinitialized the modified electrode. Results obtained using the reinitialized electrode showed good reproducibility. Furthermore, when another amyloidogenic and Cu2+-binding protein amylin was used as the target, no voltammetric response was observed. These results indicate that the AFPP-modified electrode provides a promising, label-free, sensitive, selective, cost-effective, and easy method for the quantification of Aβ.
机译:摘要淀粉样β肽(Aβ)被认为是阿尔茨海默氏病早期诊断的重要生物标志物。因此,人们渴望有实用且可靠的方法来测定Aβ水平。在这项研究中,开发了一种快速,灵敏和选择性的电化学方法,用于在肽修饰的金电极上使用Cu2 +氧化还原循环检测Aβ(1–40)。可以促进Aβ纤维化(AFPP)的19个残基肽被固定在金电极上。将Aβ溶液与修饰电极孵育1小时后,添加Cu2 +溶液并进行循环伏安法测量。发现伏安响应与Aβ(1–40)浓度在0.1–5μM范围内成比例,检测限达到18 nM。用氢氧化钠和乙二胺四乙酸盐溶液洗涤很容易重新初始化修饰的电极。使用重新初始化的电极获得的结果显示出良好的重现性。此外,当另一个淀粉样蛋白生成和Cu 2+结合蛋白淀粉样蛋白用作靶标时,未观察到伏安反应。这些结果表明,AFPP修饰的电极为Aβ的定量提供了一种有前途的,无标记,灵敏,选择性,成本有效且简便的方法。

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