Dissecting the assembly of Aβ16-22 amyloid peptides into antiparallel β sheets

Citations of this article
Mendeley users who have this article in their library.


Multiple long molecular dynamics simulations are used to probe the oligomerization mechanism of Aβ16-22 (KLVFFAE) peptides. The peptides, in the monomeric form, adopt either compact random-coil or extended β strand-like structures. The assembly of the low-energy oligomers, in which the peptides form antiparallel β sheets, occurs by multiple pathways with the formation of an obligatory α-helical intermediate. This observation and the experimental results on fibrillogenesis of Aβ1-40 and Aβ1-42 peptides suggest that the assembly mechanism (random coil → α helix → β strand) is universal for this class of peptides. In Aβ16-22 oligomers both interpeptide hydrophobic and electrostatic interactions are critical in the formation of the antiparallel β sheet structure. Mutations of either hydrophobic or charged residues destabilize the oligomer, which implies that the 16-22 fragments of Arctic (E22G), Dutch (E22Q), and Italian (E22K) mutants are unlikely to form ordered fibrils.




Klimov, D. K., & Thirumalai, D. (2003). Dissecting the assembly of Aβ16-22 amyloid peptides into antiparallel β sheets. Structure, 11(3), 295–307. https://doi.org/10.1016/S0969-2126(03)00031-5

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free