Affiliations 

  • 1 Department of Neurosurgery, Shandong Provincial Hospital Affiliated to Shandong University, No.324, Jingwu Road, Huaiyin District, Jinan, Shandong, 250021, PR China
  • 2 Department of Obstetrics, Shandong Provincial Hospital Affiliated to Shandong University, Jinan, Shandong, 250021, PR China
  • 3 Department of Biological Engineering, College of Engineering, Inha University, Incheon, 402-751, Republic of Korea
  • 4 Institute of Nano Electronic Engineering, Universiti Malaysia Perlis, 01000, Kangar, Perlis, Malaysia; School of Bioprocess Engineering, Universiti Malaysia Perlis, 02600, Arau, Perlis, Malaysia. Electronic address: subash@unimap.edu.my
  • 5 Department of Neurosurgery, The First Affiliated Hospital of Shandong First Medical University, Jinan, 250001, Shandong, China; Department of Neurosurgery, Jiangxi Provincial People's Hospital Affiliated to Nanchang University, No.92, Aiguo Road, Nanchang, Jiangxi, 330006, China. Electronic address: drxintao@yeah.net
Anal Chim Acta, 2020 Jan 15;1094:142-150.
PMID: 31761041 DOI: 10.1016/j.aca.2019.10.012

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.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.