Analytical and Bioanalytical Chemistry

, Volume 405, Issue 17, pp 5725–5741

Advances in electrochemical detection for study of neurodegenerative disorders

Review

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

Abstract

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.

https://static-content.springer.com/image/art%3A10.1007%2Fs00216-013-6904-3/MediaObjects/216_2013_6904_Figa_HTML.gif
Figure

Keywords

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