title: Advances in electrochemical detection for study of neurodegenerative disorders.
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.
authors.affiliation: Department of Physical and Environmental Sciences, University of Toronto Scarborough, 1265 Military Trail, Scarborough, ON, M1C 1A4, Canada.
authors.forename: Anthony
authors.initials: A
authors.lastname: Veloso
authors.forename: Kagan
authors.initials: K
authors.lastname: Kerman
mesh_terms: D055664:Electrochemical Techniques / Q000379:methods*; D006801:Humans; D019636:Neurodegenerative Diseases / Q000175:diagnosis* / Q000378:metabolism; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D011506:Proteins