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Advances in electrochemical detection for study of neurodegenerative disorders

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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.

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  1. Department of Physical and Environmental Sciences, University of Toronto Scarborough, 1265 Military Trail, Scarborough, ON, M1C 1A4, Canada

    Anthony Veloso & Kagan Kerman

  2. Department of Chemistry, University of Toronto, 80 St. George Street, Toronto, ON, M5S 3H6, Canada

    Anthony Veloso & Kagan Kerman

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Veloso, A., Kerman, K. Advances in electrochemical detection for study of neurodegenerative disorders. Anal Bioanal Chem 405, 5725–5741 (2013). https://doi.org/10.1007/s00216-013-6904-3

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