3 years ago

X-ray Crystallographic Structure of a Compact Dodecamer from a Peptide Derived from Aβ16–36

X-ray Crystallographic Structure of a Compact Dodecamer from a Peptide Derived from Aβ16–36
James S. Nowick, Ryan K. Spencer, Patrick J. Salveson, Adam G. Kreutzer
The assembly of the β-amyloid peptide, Aβ, into soluble oligomers is associated with neurodegeneration in Alzheimer’s disease. The Aβ oligomers are thought to be composed of β-hairpins. Here, the effect of shifting the residue pairing of the β-hairpins on the structures of the oligomers that form is explored through X-ray crystallography. Three residue pairings were investigated using constrained macrocyclic β-hairpins in which Aβ30–36 is juxtaposed with Aβ17–23, Aβ16–22, and Aβ15–21. The Aβ16–22–Aβ30–36 pairing forms a compact ball-shaped dodecamer composed of fused triangular trimers. This dodecamer may help explain the structures of the trimers and dodecamers formed by full-length Aβ.

Publisher URL: http://dx.doi.org/10.1021/acs.orglett.7b01445

DOI: 10.1021/acs.orglett.7b01445

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