Intact amyloid-β peptides (Aβ) may undergo prion-like aggregation when they interact with chemically or structurally modified variants of Aβ present in extracellular pathohistological inclusions (amyloid plaques). This aggregation is regarded as one of the key molecular mechanisms of Alzheimer's disease (AD) pathogenesis. Zinc ions are involved in the pathological dimerization and oligomerization of natural Aβ isoforms, and zinc-induced oligomers can also initiate the pathological aggregation of Aβ. Based on the earlier found molecular mechanism of zinc-dependent oligomerization of Aβ, it has been suggested that the targeted inhibition of the 11EVHH14 site in one Aβ molecule from zinc-mediated interactions with the same site of another Aβ molecule can effectively inhibit the oligomerization and aggregation of Aβ. Taking into account the similarity in the structural organization of zinc-binding sites within Aβ and angiotensin-converting enzyme (ACE), we hypothesized that inhibitors of the ACE active sites could specifically interact with the 11EVHH14 site of Aβ. Using a surface plasmon resonance biosensor and nuclear magnetic resonance spectroscopy, we have found that the ACE inhibitor enalaprilat effectively inhibits zinc-dependent dimerization of the metal-binding domains of intact Aβ and Aβ with isomerized Asp7 (isoAβ). We have also found that enalaprilat protects SH-SY5Y human neuroblastoma cells from the toxic effects of Aβ(1-42) and isoAβ(1-42), which are among the most common components of amyloid plaques. The results confirm the role of zincdependent oligomerization of Aβ in AD pathogenesis and make it possible one to consider enalaprilat as a prototype of antiaggregation agents for treating AD.