Beyond AChE, we show thatthe stereoelectronic requirements imposedby the AChE gorge for multisite binding have a templating effect thatleads to compounds that are active in other key biological targetsin AD and other neurological and non-neurological diseases, such asBACE-1 and the aggregation of amyloidogenic proteins (β-amyloid,tau, α-synuclein, prion protein, transthyretin, and human isletamyloid polypeptide). This evidence concerns the gene TTR and Alzheimer disease.