ACHE and nervous system disorder: By using E. coli cellsgenetically modified to separately express 13 amyloid-prone proteins(Figure 12 legend),involved in neurological and non-neurological diseases, as well asfungal, yeast, and bacterial amyloidogenic proteins, we found thatthe multisite AChE inhibitors DP128 and (−)-HUP7TH block theaggregation of all of the tested amyloidogenic proteins, with similarpotencies (50–85% and 40–80%, respectively, at 10 μM).47 In contrast, the CAS inhibitor huprine Y wasessentially inactive against all amyloids.