Cu2+ Affects Amyloid-β (1–42) Aggregation by Increasing Peptide-Peptide Binding Forces
Figure 6
Proposed structures of Aβ dimers with and without copper assembled from stable Aβ(1–42) monomer structures.
Each monomer has an internal antiparallel β-sheet between residues 18–21 and 30–33. The dimers are assembled by juxtaposition of the self-recognition site residues 18–21 in antiparallel (A, C) and parallel (B, D) orientation. Both orientations bring His6, His13 and His14 of each monomer into close proximity, requiring little reorientation to bind Cu2+ ions (filled green circles). Structures are courtesy of D. F. Raffa and A. Rauk, Molecular Dynamics Study of the Beta Amyloid Peptide of Alzheimer's Disease and its Divalent Copper Complexes [53], created using Raswin software.