Effects of N-Terminal Residues on the Assembly of Constrained β-Hairpin Peptides Derived from Aβ.

ABSTRACT: This paper describes the synthesis, solution-phase biophysical studies, and X-ray crystallographic structures of hexamers formed by macrocyclic β-hairpin peptides derived from the central and C-terminal regions of Aβ, which bear "tails" derived from the N-terminus of Aβ. Soluble oligomers of the β-amyloid peptide, Aβ, are thought to be the synaptotoxic species responsible for neurodegeneration in Alzheimer's disease. Over the last 20 years, evidence has accumulated that implicates the N-terminus of Aβ as a region that may initiate the formation of damaging oligomeric species. We previously studied, in our laboratory, macrocyclic β-hairpin peptides derived from Aβ_16-22 and Aβ_30-36, capable of forming hexamers that can be observed by X-ray crystallography and SDS-PAGE.

SUBMITTER: Samdin TD 

PROVIDER: S-EPMC7927569 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature