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基于金纳米壳种子的单壁碳纳米管在伏安传感器上用于诊断神经退行性帕金森病。

Gold-nanourchin seeded single-walled carbon nanotube on voltammetry sensor for diagnosing neurogenerative Parkinson's disease.

机构信息

Department of Neurosurgery, Shandong Provincial Hospital Affiliated to Shandong University, No.324, Jingwu Road, Huaiyin District, Jinan, Shandong, 250021, PR China.

Department of Obstetrics, Shandong Provincial Hospital Affiliated to Shandong University, Jinan, Shandong, 250021, PR China.

出版信息

Anal Chim Acta. 2020 Jan 15;1094:142-150. doi: 10.1016/j.aca.2019.10.012. Epub 2019 Oct 12.

Abstract

α-synuclein is a predominantly expressing neuronal protein for understanding the neurodegenerative disorders. A diagnosing system with aggregated α-synuclein encoded by SNCA gene is necessary to make the precautionary treatment against Parkinson's disease (PD). Herein, gold-nanourchin conjugated anti-α-synuclein antibody was desired as the probe and seeded on single-walled carbon nanotube (SWCN) integrated interdigitated electrode (IDE). The surface morphology of SWCN-modified IDE and gold urchin-antibody conjugates were observed under FESEM, FETEM and AFM, the existing elements were confirmed. Voltammetry analysis revealed that the limit of fibril-formed α-synuclein detection was improved by 1000 folds (1 fM) with gold-nanourchin-antibody modified surface, compared to the surface with only antibody (1 pM). Validating the interaction of α-synuclein by Enzyme-linked Immunosorbent Assay was displayed the detection limit as 10 pM. IDE has a good reproducibility and a higher selectivity on α-synuclein as evidenced by the interactive analysis with the control proteins, PARK1 and DJ-1.

摘要

α-突触核蛋白是一种主要表达于神经元的蛋白质,对于理解神经退行性疾病具有重要意义。为了对帕金森病(PD)进行预防性治疗,需要建立一种基于 SNCA 基因编码的聚集态 α-突触核蛋白的诊断系统。在此,我们希望将金纳米刺修饰的抗 α-突触核蛋白抗体用作探针,并将其接种在单壁碳纳米管(SWCN)集成的叉指电极(IDE)上。通过 FESEM、FETEM 和 AFM 观察 SWCN 修饰的 IDE 和金纳米刺-抗体缀合物的表面形貌,确认了存在的元素。伏安分析表明,与仅抗体修饰的表面(1 pM)相比,金纳米刺-抗体修饰的表面将纤维形成的 α-突触核蛋白检测的检测限提高了 1000 倍(1 fM)。通过酶联免疫吸附试验验证了 α-突触核蛋白的相互作用,显示检测限为 10 pM。IDE 具有良好的重现性和更高的 α-突触核蛋白选择性,这一点通过与对照蛋白 PARK1 和 DJ-1 的相互作用分析得到了证明。

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