A rationally designed oligomerization inhibitor interacts with early intermediate assemblies of amyloid‐β polypeptide (Aβ) through the aromatic elements and inhibits their assembly into the toxic oligomers that cause Alzheimer's disease by a unique Cα‐methylation β‐breakage strategy. The electrostatic potential of the low‐energy conformation of the dipeptide inhibitor bound to Aβ is shown.
The accumulation of amyloid‐β (Aβ) as amyloid fibril deposits may play a central role in the pathogenesis of Alzheimer's disease, which is among the most common diseases of the 21st century. E. Gazit and co‐workers describe in their Communication on page 1981 ff. a novel Aβ fibrilization inhibitor, whose mechanism of action is based on targeting aromatic recognition modules together with a unique Cα‐methylation β‐breakage strategy. We thank Tal Mazor for the graphical assistance with the cover.
