Formation of polymorphic amyloid fibrils is a common feature in neurodegenerative
diseases involving protein aggregation. In Alzheimer's disease, different fibril structures may …

Despite years of intensive research, little is known about oligomeric structures present
during Alzheimer's disease (AD). Excess of amyloid beta (Aβ) peptides and their …

Background Misfolding and self-assembly of Amyloid-β (Aβ) peptides into amyloid fibrils is
pathologically linked to the development of Alzheimer's disease. Polymorphic Aβ structures …

Elucidating the structure of Aβ1− 40 fibrils is of interest in Alzheimer's disease research
because it is required for designing therapeutics that target Aβ1− 40 fibril formation at an …

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 …

Alzheimer's disease is the most fatal neurodegenerative disorder characterized by the
aggregation and deposition of Amyloid β (Aβ) oligomers in the brain of patients. Two …

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 …

The aggregation of amyloid-β 42 (Aβ 42) peptide into toxic oligomers and fibrils is a key step
in the Alzheimer disease pathogenesis. The recent studies highlighted that lysine residues …

The self-assembly of amyloid-β (Aβ) peptides into senile plaques in the brain is a hallmark of
Alzheimer's disease (AD) pathology. Mutation and histidine tautomerism are considered …

Alzheimer's disease (AD) is associated with the oligomerization and/or fibrillation of amyloid
beta (Aβ) peptides, which cause damage to brain cells. Aβ oligomers and fibrils contain …