Aggregation of amyloid beta peptide (A?) and inflammatory processes associated with the generation of superoxide, hydrogen peroxide, and hydroxyl radicals are responsible for neurotoxicity in Alzheimer?s disease. The latter are a result of the redox activity of copper-bound A? complexes with molecular oxygen. A ligand (PI1), previously designed to compete with A? for copper, and a pseudopeptide (SGC1) with a property of breaking the self-aggregation of A?, are attached to each other to form a new pseudopeptide (TGC1) in this study. Using a combination of density functional theory and molecular dynamics simulations, we show that TGC1 should have the ability to inhibit self-aggregation of A?, prevent the binding of copper to A?, and quench the redox activity of the copper. This trifunctional ligand is a good candidate for development into an anti-Alzheimer drug.