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 …

Although the Aβ37–42 peptide has two opposite terminal charges, counterintuitively its
current fibril amyloid structure reveals in register parallel β-strands, as formed by the full …

Amyloid-β (Aβ) oligomers play a central role in Alzheimer's disease (AD). Plaques of AD
patients consist of Aβ40 and Aβ42 peptides and truncated Aβ peptides. The Aβ24 peptide …

The amyloid-β (Aβ) peptide is one key molecule in the pathogenesis of Alzheimer's disease.
We investigated the conformational stability of a nonfibrillar tetrameric Aβ structure by …

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 …

Aβ 16–22 is believed to have critical role in early aggregation of full length amyloids that are
associated with the Alzheimer's disease and can aggregate to form amyloid fibrils. However …

The aggregation of amyloid-β protein (Aβ) into oligomers and amyloid fibrils is closely
related to Alzheimer's disease (AD). Aβ40 and Aβ42, as two most prominent isoforms of Aβ …

Amyloid β (Aβ) peptides are a primary component of fibrils and oligomers implicated in the
etiology of Alzheimer's disease (AD). However, the intrinsic flexibility of these peptides has …

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 …

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