The self-assembly and fibrillation of amyloid β (Aβ) proteins is the neuropathological
hallmark of Alzheimer's disease. However, the molecular mechanism of how disordered …

The 25–35 fragment of the Alzheimer amyloid β (Aβ) peptide is a naturally occurring
proteolytic by-product that retains the toxicity of its larger, better-known counterpart, Aβ (1 …

Alzheimer's disease (AD) is associated with the aberrant self-assembly of amyloid-β (Aβ)
protein into fibrillar deposits. The disaggregation of Aβ fibril is believed as one of the major …

Recent experimental data demonstrate that small, soluble amyloid− β42 oligomers play an
important role in Alzheimer's disease because they exhibit neurotoxic properties and also …

In present study, we set out to investigate the conformation dynamics of Aβ40 and Aβ42
through exploring the impact of intra-molecular interactions on conformation dynamics using …

The self-assembly of the amyloid-β (Aβ) peptide of 39–43 amino acids into senile plaques is
one hallmark of Alzheimer's disease (AD) pathology. While A2 V carriers remain healthy in …

The aggregation cascade and peptide-membrane interactions of the amyloid β-peptide (Aβ)
have been implicated as toxic events in the development and progression of Alzheimer's …

Combined results of theoretical molecular dynamic simulations and in vitro spectroscopic
(circular dichroism and fluorescence) studies are presented, providing the atomistic and …

Alzheimer's disease (AD) is an irreversible, progressive, and degenerative brain disorder
characterized by the aggregation and deposition of amyloid-β (Aβ) oligomers in the brain of …

Self-assembly of the 40/42 amino acid Aβ peptide is a key player in Alzheimer's disease.
Aβ40 is the most prevalent species, while Aβ42 is the most toxic. It has been suggested that …