Alzheimer's disease amyloid beta peptides in vitro electrochemical oxidation.

The oxidative behaviour of the human amyloid beta (Aβ1-40 and Aβ1-42) peptides and a group of similar peptides: control inverse (Aβ40-1 and Aβ42-1), mutants (Aβ1-40Phe10 and Aβ1-40Nle35), rat Aβ1-40Rat, and fragments (Aβ1-28, Aβ1-16, Aβ10-20, Aβ12-28, and Aβ17-42), in solution or adsorbed, at a glassy carbon electrode, by cyclic and differential pulse voltammetry, were investigated and compared. Structurally the Aβ1-40 and Aβ1-42 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.