Analytical and Bioanalytical Chemistry

, Volume 405, Issue 17, pp 5725–5741

Advances in electrochemical detection for study of neurodegenerative disorders


DOI: 10.1007/s00216-013-6904-3

Cite this article as:
Veloso, A. & Kerman, K. Anal Bioanal Chem (2013) 405: 5725. doi:10.1007/s00216-013-6904-3


Several severe neurodegenerative disorders, including Alzheimer’s disease, Parkinson’s disease, and prion-associated transmissible spongiform encephalopathies, have been linked to dysregulation of specific proteins capable of self-assembly into deleterious fibrillar aggregates termed amyloids. A wide range of analytical techniques has been used to clarify the mechanisms of these protein-misfolding processes, in the hope of developing effective therapeutic treatment. Most of these studies have relied heavily on conventional methods of protein characterization, notably circular dichroism spectroscopy, thioflavin T fluorescence, transmission electron microscopy, and atomic force microscopy, which are particularly suitable for monitoring later-stage aggregate formation. Although electrochemical methods of protein detection have existed for some time, they have only recently gained prominence as a powerful tool for studying the early stages of protein aggregation during which the more toxic soluble amyloid species form. Electrochemical detection methods include direct detection of intrinsic redox-active amino acid residues, protein-catalyzed hydrogen evolution, use of extrinsic β-sheet binding mediators, and impedance spectroscopy. In this review, we evaluate the use of electrochemistry for study of protein aggregation related to neurodegenerative disorders.


Amyloid aggregationPrionElectrochemicalTyrosine oxidationPeak HImpedance spectroscopy

Copyright information

© Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  1. 1.Department of Physical and Environmental SciencesUniversity of Toronto ScarboroughScarboroughCanada
  2. 2.Department of ChemistryUniversity of TorontoTorontoCanada