Figure 10. Comparison of hIAPP structures.

(a) Known structures and models of hIAPP suggest partial folding of the monomeric subunit, although the folding varies with the sample preparation and environment. (b) Monomeric hIAPP prepared at pH 5.3 demonstrates a partial helical fold spanning C7-F15 (PDB: 5MGQ) (Rodriguez Camargo et al., 2017). (c) Monomeric hIAPP stabilized by SDS micelles adopts a similar N-terminal helix and a second helical region near the C-terminus (PDB: 2L86) (Nanga et al., 2011). (d) The striated ribbon morphology of hIAPP fibers shows twoβ-hairpins interacting through their C-terminal β-strands (Luca et al., 2007). (e) The folded hIAPP monomer interacting with the surface of ND1 possesses three antiparallel β-strands.