The water-soluble hydrophilic part of human A beta peptide has been extended to include a C-terminal cysteine residue. Utilizing the thiol functionality of this cysteine residue, self-assembled monolayers (SAM) of these peptides are formed on Au electrodes. Atomic force microscopy imaging confirms formation of small A beta aggregates on the surface of the electrode. These aggregates bind redox active metals like Cu and cofactors like heme, both of which are proposed to generate toxic partially reduced oxygen species (PROS) and play a vital role in Alzheimer's disease. The spectroscopic and electrochemical properties of these Cu and heme bound A beta SAM are similar to those reported for the soluble Cu and heme bound A beta peptide. Experiments performed on these A beta-SAM electrodes clearly demonstrate that (1) heme bound A beta is kinetically more competent in reducing O-2 than Cu bound A beta, (2) under physiological conditions the, reduced Cu site produces twice as much PROS (measured in situ) than the reduced heme site, and (3) chelators like clioquinol remove Cu from these aggregates, while drugs like methylene blue inhibit O-2 reactivity of the heme cofactor. This artificial.; construct provides a very easy platform for investigating potential drugs affecting aggregation of human A beta peptides and PROS generation by its complexes with redox active metals and cofactors