β-amyloid (Aβ) is comprised of a group of peptides formed as a result of cleavage of the amyloid precursor protein by secretases. Aβ aggregation is considered as a central event in pathogenesis of Alzheimer's disease, the most common human neurodegenerative disorder. Molecular mechanisms of Aβ aggregation have intensively being investigated using synthetic Aβ peptides by methods based on monitoring of aggregates, including determination of their size and structure. In this review, an orthogonal approach to the study of Aβ aggregation is considered, which relies on electrochemical registration of the loss of peptide monomers. Electrochemical analysis of Aβ (by voltammetry and amperometric flow injection analysis) is based on registration of the oxidation signal of electroactive amino acid residues of the peptide on an electrode surface. The Aβ oxidation signal disappears, when the peptide is included in the aggregate. The advantages and disadvantages of electrochemical analysis for the study of spontaneous and metal-induced aggregation of Aβ, comparative analysis of various peptide isoforms, and study of the process of complexation of metal ions with the metal-binding domain of Aβ are discussed. It is concluded that the combined use of the electrochemical method and the methods based on detection of Aβ aggregates makes it possible to obtain more complete information about the mechanisms of peptide aggregation.
Keywords: Alzheimer’s disease; aggregation; electrochemical oxidation; electrochemistry; β-amyloid.