论文部分内容阅读
The pathogenesis of Alzheimers disease(AD)is associated with the abnormal self-assembly of the amyloid-β(Aβ)peptide into toxic aggregates with β-sheet character.The inhibition of β-sheet formation has been considered as the primary therapeutic strategy for the AD.Increasing data show that hydrophobic nanoparticles retard Aβ fibrillization by slowing down the nucleation process.However,the detailed effects of these nanoparticles on the structures of the early formed Aβ oligomers remain elusive.In this study,we investigate the conformations of Aβ(16-22)octamers in the absence and presence of a typical hydrophobic nanoparticle:single-walled carbon nanotube(SWCNT)and Au nanoparticles(AuN)by all-atom replica exchange molecular dynamics(REMD)simulations and molecular dynamics(MD)in explicit solvent.