Figure 1.

Diverse morphologies of protein aggregates. (A) The characteristic amyloid cross-β structure, as seen in a fibril model of the Iowa mutant (D23N) of Aβ₄₀ (PDB ID: 2lnq (Qiang et al., 2012)). Individual polypeptide chains are colored differently. (B) From left to right: transmission electron microscopy images of Aβ₄₂ oligomers, protofibrils, and fibrils. Reprinted by permission from Ahmed et al. (2010), copyright 2010 Macmillan Publishers Ltd. (C) Atomic force microscopy (AFM) images of Aβ₄₀ (left) and α-synuclein (middle) incubated with lipid bilayers. Inset shows a lipid bilayer in the absence of peptide/protein. Scale bar, 100 nm. At right, high-resolution AFM images (image size: 25 nm) showing individual pores formed by Aβ₄₀ and α-synuclein within lipid bilayers. Reprinted from Quist et al. (2005), copyright 2005 National Academy of Sciences, USA.