Biophysical properties of the fibril structure of the toxic conformer of amyloid-β42: Characterization by atomic force microscopy in liquid and molecular docking

R Biyani, K Hirata, K Oqmhula… - … Applied Materials & …, 2023 - ACS Publications
Alzheimer's disease is associated with the aggregation of the misfolded neuronal peptide,
amyloid-β42 (Aβ42). Evidence has suggested that several reasons are responsible for the …

[HTML][HTML] Assemblies of amyloid-β30–36 hexamer and its G33V/L34T mutants by replica-exchange molecular dynamics simulation

Z Qian, Q Zhang, Y Liu, P Chen - PLoS One, 2017 - journals.plos.org
The aggregation of amyloid-β peptides is associated with the pathogenesis of Alzheimer's
disease, in which the 30–36 fragments play an important part as a fiber-forming hydrophobic …

Amino acid substitutions [K16A] and [K28A] distinctly affect amyloid β-protein oligomerization

M Žganec, N Kruczek, B Urbanc - Journal of biological physics, 2016 - Springer
Amyloid β-protein (A β) assembles into oligomers that play a seminal role in Alzheimer's
disease (AD), a leading cause of dementia among the elderly. Despite undisputed …

[HTML][HTML] Role of β-hairpin formation in aggregation: the self-assembly of the amyloid-β (25–35) peptide

L Larini, JE Shea - Biophysical journal, 2012 - cell.com
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 …

Conformational Ensemble and Polymorphism of the All-Atom Alzheimer's Aβ37–42 Amyloid Peptide Oligomers

PH Nguyen, P Derreumaux - The Journal of Physical Chemistry B, 2013 - ACS Publications
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 …

Key residue for aggregation of amyloid-β peptides

SG Itoh, M Yagi-Utsumi, K Kato… - ACS Chemical …, 2022 - ACS Publications
It is known that oligomers of amyloid-β (Aβ) peptide are associated with Alzheimer's disease.
Aβ has two isoforms: Aβ40 and Aβ42. Although the difference between Aβ40 and Aβ42 is …

Effect of Piedmont mutation (L34V) on the structure, dynamics, and aggregation of Alzheimer's Aβ40 peptide

RK Saini, H Thakur, B Goyal - Journal of Molecular Graphics and Modelling, 2020 - Elsevier
The amyloid-β (Aβ) aggregation in the brain has been associated with the development of
Alzheimer's disease (AD). The previous studies have reported that Piedmont mutation …

Elucidation of amyloid β-protein oligomerization mechanisms: discrete molecular dynamics study

B Urbanc, M Betnel, L Cruz, G Bitan… - Journal of the American …, 2010 - ACS Publications
Oligomers of amyloid β-protein (Aβ) play a central role in the pathology of Alzheimer's
disease. Of the two predominant Aβ alloforms, Aβ1− 40 and Aβ1− 42, Aβ1− 42 is more …

The structures of the E22Δ mutant-type amyloid-β alloforms and the impact of E22Δ mutation on the structures of the wild-type amyloid-β alloforms

O Coskuner, O Wise-Scira, G Perry… - ACS Chemical …, 2013 - ACS Publications
Structural differences between the intrinsically disordered fibrillogenic wild-type Aβ40 and
Aβ42 peptides are linked to Alzheimer's disease. Recently, the E22Δ genetic missense …

[HTML][HTML] Aggregation mechanism of Alzheimer's amyloid β-peptide mediated by α-strand/α-sheet structure

A Balupuri, KE Choi, NS Kang - International Journal of Molecular …, 2020 - mdpi.com
Alzheimer's disease (AD) is one of the most common neurodegenerative diseases and a
widespread form of dementia. Aggregated forms of the amyloid β-peptide (Aβ) are identified …