To study the early stage of amyloid‐β peptide (Aβ) aggregation, hexamers of the wild‐type
(WT) Aβ16–35 and its mutants with amyloid‐like conformations have been studied by …

Abstract The 16–22 amino-acid fragment of the β-amyloid peptide associated with the
Alzheimer's disease, Aβ, is capable of forming amyloid fibrils. Here we study the aggregation …

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 …

Several neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's
diseases are associated with amyloid fibrils formed by different polypeptides. We probe the …

Aggregates of the amyloid-β (Aβ) peptide are implicated as a causative substance in
Alzheimer's disease. Molecular dynamics simulations provide valuable contributions for …

Recent experiments have shown that the Taiwan mutation (D7H) slows the fibril formation of
amyloid peptides Aβ40 and Aβ42. Motivated by this finding, we have studied the influence of …

To study the folding/unfolding properties of a β-amyloid peptide Aβ12–36 of Alzheimer's
disease, five molecular dynamics simulations of Aβ12–36 in explicit water were done at 450 …

Amyloid-β (Aβ) peptides exhibit many distinct structural morphology at the early aggregate
stage, some of which are biological relevant to the pathogenesis of Alzheimer's disease …

The mechanisms of deposition and dissociation are implicated in the assembly of amyloid
fibrils. To investigate the kinetics of unbinding of Aβ16–22 monomers from preformed fibrils …

The amyloid β-peptides (Aβs), containing 39–43 residues, are the key protein components
of amyloid deposits in Alzheimer's disease. To structurally characterize the dynamic …