Mechanistic insight into E22Q-mutation-induced antiparallel-to-parallel β-sheet transition of Aβ 16− 22 fibrils: an all-atom simulation study
Alzheimer's disease is associated with the abnormal self-assembly of amyloid-β (Aβ)
peptide into toxic oligomers and fibrils. Recent experiments reported that Aβ16− 22 …
peptide into toxic oligomers and fibrils. Recent experiments reported that Aβ16− 22 …
[HTML][HTML] Structure of ring-shaped Aβ42 oligomers determined by conformational selection
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 …
critical role in the pathogenesis of Alzheimer's disease. However, it has been challenging to …
Effect of the English familial disease mutation (H6R) on the monomers and dimers of Aβ40 and Aβ42
MH Viet, PH Nguyen, P Derreumaux… - ACS chemical …, 2014 - ACS Publications
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 …
Alzheimer's disease. Recent experiments have shown that the English familial disease …
[HTML][HTML] Unfolding of the amyloid β-peptide central helix: mechanistic insights from molecular dynamics simulations
Alzheimer's disease (AD) pathogenesis is associated with formation of amyloid fibrils
caused by polymerization of the amyloid β-peptide (Aβ), which is a process that requires …
caused by polymerization of the amyloid β-peptide (Aβ), which is a process that requires …
Aβ (16–22) peptides can assemble into ordered β-barrels and bilayer β-sheets, while substitution of phenylalanine 19 by tryptophan increases the population of …
L Xie, Y Luo, G Wei - The Journal of Physical Chemistry B, 2013 - ACS Publications
A recent experimental study reported that termini-uncapped Aβ (16–22)(with sequence
KLVFFAE) peptides self-assembled into nanofibrils at pH 2.0. The oligomerization of this …
KLVFFAE) peptides self-assembled into nanofibrils at pH 2.0. The oligomerization of this …
Effect of familial mutations on the interconversion of α-Helix to β-sheet structures in an amyloid-forming peptide: insight from umbrella sampling simulations
Understanding the initial events of aggregation of amyloid β monomers to form β-sheet rich
fibrils is useful for the development of therapeutics for Alzheimer's disease. In this context …
fibrils is useful for the development of therapeutics for Alzheimer's disease. In this context …
Insights into the baicalein-induced destabilization of LS-shaped Aβ 42 protofibrils using computer simulations
G Kaur, OK Mankoo, A Kaur, D Goyal… - Physical Chemistry …, 2024 - pubs.rsc.org
Amyloid-β (Aβ) peptides aggregate spontaneously into various aggregating species
comprising oligomers, protofibrils, and mature fibrils in Alzheimer's disease (AD). Disrupting …
comprising oligomers, protofibrils, and mature fibrils in Alzheimer's disease (AD). Disrupting …
The conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length
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 …
We investigated the conformational stability of a nonfibrillar tetrameric Aβ structure by …
Molecular mechanism of misfolding and aggregation of Aβ (13–23)
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 …
molecular signature of the development of Alzheimer's disease, but molecular mechanisms …
Zn2+ Binding Increases Parallel Structure in the Aβ(16–22) Oligomer by Disrupting Salt Bridge in Antiparallel Structure
Y Song, M Wu, C Wang, H Fang… - The Journal of Physical …, 2024 - ACS Publications
The aggregation of monomeric amyloid β protein (Aβ) into oligomers and amyloid plaque in
the brain is associated with Alzheimer's disease. The hydrophobic central core Aβ16–22 has …
the brain is associated with Alzheimer's disease. The hydrophobic central core Aβ16–22 has …