Alzheimer's disease (AD) is one of the most common dementia. The aggregation and
deposition of the amyloid-β peptide (Aβ) in neural tissue is its characteristic symptom. To …

The self-aggregation of amyloid-β (Aβ) and tau proteins are closely implicated in Alzheimer's
disease (AD). Recent evidence indicates that Aβ and tau proteins can cross-interact to form …

Recent studies suggest that soluble oligomers of amyloid-forming peptides have toxic effects
in cell cultures. In this study, the folding of three Alzheimer's A β16-22 peptides have been …

Amyloid β (Aβ) monomers are the smallest assembly units, and play an important role in
most of the individual processes involved in amyloid fibril formation. An important question is …

We investigate Aβ 17-42 protofibril structures in solution using molecular dynamics
simulations. Recently, NMR and computations modeled the Aβ protofibril as a longitudinal …

Using replica exchange molecular dynamics, we study the effect of Asp23Tyr mutation on
Aβ10− 40 fibril growth. The effect of this mutation is revealed through the computation of free …

Formation of intracellular plaques and small oligomeric species of amyloid β (Aβ) peptides
inside neurons is a hallmark of Alzheimer's disease. The most abundant Aβ species in the …

Amyloid beta (Aβ) oligomerization is associated with the origin and progression of
Alzheimer's disease (AD). While the A2V mutation enhances aggregation kinetics and …

The aggregation of amyloid‐β (Aβ) peptide has been associated with the pathogenesis of
Alzheimer disease. The recent studies highlighted that L17A/F19A double mutation …

Nonfibrillar neurotoxic amyloid β (Aβ) oligomer structures are typically rich in β-sheets,
which could be promoted by metal ions like Zn2+. Here, using molecular dynamics (MD) …