Alzheimer's disease amyloid beta peptides in vitro electrochemical oxidation

The oxidative behaviour of the human amyloid beta (Aβ_1-40 and Aβ_1-42) peptides and a group of similar peptides: control inverse (Aβ_40-1 and Aβ_42-1), mutants (Aβ_1-40Phe¹⁰ and Aβ_1-40Nle³⁵), rat Aβ_1-40Rat, and fragments (Aβ_1-28, Aβ_1-16, Aβ_10-20, Aβ_12-28, and Aβ_17-42), in solution or adsorbed, at a glassy carbon electrode, by cyclic and differential pulse voltammetry, were investigated and compared. Structurally the Aβ_1-40 and Aβ_1-42 sequences contain five electroactive amino acid residues, one tyrosine (Tyr¹⁰), three histidines (His⁶, His¹³ and His¹⁴) and one methionine (Met³⁵). The Aβ peptide 3D structure influenced the exposure of the redox residues to the electrode surface and their oxidation peak currents. Depending on the amino acid sequence length and content, the Aβ peptides gave one or two oxidation peaks. The first electron transfer reaction corresponded to the tyrosine amino acid residue oxidation, and the second to both histidines and methionine amino acid residues. The highest contribution to the second oxidation peak current was from His¹³, followed by His¹⁴ and His⁶ residues, and Met³⁵ residue had the lowest contribution. The Aβ peptides electron transfer depended on peptide hydrophobicity and 3D structure, the redox residues position in the sequence, the redox residues close to N-termini giving the highest oxidation peak currents.