Analysis of the stabilities of hexameric amyloid-β(1-42) models using discrete molecular dynamics simulations.

ABSTRACT: Amyloid-β (Aβ) oligomers appear to play a pivotal role in Alzheimer's disease. A 42 residue long alloform, Aβ42, is closely related to etiology of the disease. In vitro results show evidences of hexamers; however structures of these hexamers have not been resolved experimentally. Here, we use discrete molecular dynamics (DMD) to analyze long duration stabilities of Aβ42 hexamer models developed previously in our lab. The hydrophobic core of these models is a six-stranded β-barrel with 3-fold radial symmetry formed by residues 30-40. This core is shielded from water by residues 1-28. The nine models we analyzed differ by the relative positions of the core β-strands, and whether the other segments surrounding the core contain α helices or β-strands. A model of an annular protofibril composed

SUBMITTER: Yun S 

PROVIDER: S-EPMC3040446 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature