Role of β-hairpin formation in aggregation: the self-assembly of the amyloid-β(25-35) peptide.

ABSTRACT: The amyloid-β(25-35) peptide plays a key role in the etiology of Alzheimer's disease due to its extreme toxicity even in the absence of aging. Because of its high tendency to aggregate and its low solubility in water, the structure of this peptide is still unknown. In this work, we sought to understand the early stages of aggregation of the amyloid-β(25-35) peptide by conducting simulations of oligomers ranging from monomers to tetramers. Our simulations show that although the monomer preferentially adopts a β-hairpin conformation, larger aggregates have extended structures, and a clear transition from compact β-hairpin conformations to extended β-strand structures occurs between dimers and trimers. Even though β-hairpins are not present in the final architecture of the fibril, our simulat

SUBMITTER: Larini L 

PROVIDER: S-EPMC3414875 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature