The role of β-hairpins in aggregation of β-amyloid erived peptides

Alzheimer’s disease (AD) is one of the most widely recognized and prevalent neurodegenerative conditions in today’s society. However, despite its prevalence, effective pharmacological treatment is not currently available, leaving only palliative care options as the most helpful course of action. The pathogenesis of Alzheimer's disease (AD) involves the formation of proteinaceous plaques due to the aggregation of originally soluble oligomers of amyloid-β peptides [1] . These oligomers have been observed to adopt different conformations, including βsheets, α-helices, and predominantly β-hairpins. β-hairpins are capable of assuming different configurations in space. In order to investigate the mechanisms that govern β-hairpin orientation and develop an in vitro model of peptide aggregation for use in testing inhibitors of this process, two Aβ17-36 derivatives were synthesized; subsequently, their conformation was studied through circular dichroism spectroscopy (CD).