The misfolding and self-assembly of the amyloid-beta (Aβ) peptide into aggregates is a
molecular signature of the development of Alzheimer's disease, but molecular mechanisms …

The β amyloid (Aβ) peptide aggregates to form β-rich structures that are known to trigger
Alzheimer's disease. Experiments suggest that an α-helical intermediate precedes the …

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 oligomerization of amyloid beta (Aβ) peptides into soluble non-fibrillar species plays a
critical role in the pathogenesis of Alzheimer's disease. However, it has been challenging to …

Aβ (1− 40) and Aβ (1− 42) are the main forms of amyloid β (Aβ) peptides in the brain of
Alzheimer's patients; however, the latter possesses much stronger aggregation and …

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 …

The self-assembly of the amyloid beta (Aβ) peptides into senile plaques is the hallmark of
Alzheimer's disease. Recent experiments have shown that the English familial disease …

The progress toward understanding the molecular basis of Alzheimers's disease is strongly
connected to elucidating the early aggregation events of the amyloid-β (Aβ) peptide …

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 …

Intrinsically disordered peptides, such as amyloid β42 (Aβ42), lack a well-defined structure
in solution. Aβ42 can undergo abnormal aggregation and amyloidogenesis in the brain …