Constructed models of oligomeric complexes of mutated ∆K280 tau repeat R2-Aβ_17-42.

<p>The mutated ∆K280 tau repeat-R2 oligomers are based on model M1 in which hydrophobic interactions stabilize the core domain of the β-hairpins (Figure 1). Aβ_17-42 oligomers (blue) and the mutated ∆K280 tau repeat R2 oligomers (red) are organized in parallel orientation. Residue colors: Cys (brown), Ile (black), Val (green). Models H1, H2 and H3 represent single-layer conformations. In H1 and H2, the oligomers are arranged in parallel and antiparallel orientation, respectively. In H3, trimers of Aβ_17-42 and trimers of mutated ∆K280 tau repeat R2 are alternated in parallel orientation. Models H4-H7 offer four possible arrangements of double-layer conformations that differ in the interactions between C-terminus domains/N-terminus domains of each oligomer to form double-layer conformations.