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 …

[PDF][PDF] Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer

YS Lin, GR Bowman, KA Beauchamp, VS Pande - Biophysical journal, 2012 - cell.com
The aggregation of amyloid beta (Aβ) peptides plays an important role in the development of
Alzheimer's disease. Despite extensive effort, it has been difficult to characterize the …

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 …

Structural heterogeneity in familial Alzheimer's disease mutants of amyloid-beta peptides

SH Chong, J Yim, S Ham - Molecular BioSystems, 2013 - pubs.rsc.org
Alzheimer's disease is a neurodegenerative disorder characterized by progressive
deposition of amyloid-beta (Aβ) peptides in brain parenchyma and cerebral blood vessels …

Structure of ring-shaped Aβ42 oligomers determined by conformational selection

L Tran, N Basdevant, C Prévost, T Ha-Duong - Scientific reports, 2016 - nature.com
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 …

Conformational features of the Aβ 42 peptide monomer and its interaction with the surrounding solvent

P Khatua, JC Jose, N Sengupta… - Physical Chemistry …, 2016 - pubs.rsc.org
Accumulation of the amyloid beta (Aβ) peptide in the brain is responsible for debilitating
neurodegenerative diseases, such as Alzheimer's disease (AD). We have carried out …

Mechanistic insight into E22Q-mutation-induced antiparallel-to-parallel β-sheet transition of Aβ 16− 22 fibrils: an all-atom simulation study

X Li, J Lei, R Qi, L Xie, G Wei - Physical Chemistry Chemical Physics, 2019 - pubs.rsc.org
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 …

Dimerization Mechanism of Alzheimer Aβ40 Peptides: The High Content of Intrapeptide-Stabilized Conformations in A2V and A2T Heterozygous Dimers Retards …

PH Nguyen, F Sterpone, R Pouplana… - The Journal of …, 2016 - ACS Publications
Amyloid beta (Aβ) oligomerization is associated with the origin and progression of
Alzheimer's disease (AD). While the A2V mutation enhances aggregation kinetics and …

Familial Alzheimer A2 V mutation reduces the intrinsic disorder and completely changes the free energy landscape of the Aβ1–28 monomer

PH Nguyen, B Tarus, P Derreumaux - The journal of physical …, 2014 - ACS Publications
The self-assembly of the amyloid-β (Aβ) peptide of 39–43 amino acids into senile plaques is
one hallmark of Alzheimer's disease (AD) pathology. While A2 V carriers remain healthy in …

Stability of Osaka mutant and wild-type fibril models

WM Berhanu, EJ Alred… - The journal of physical …, 2015 - ACS Publications
Single amino acid mutations in amyloid-beta (Aβ) peptides can lead to early onset and
increased severity of Alzheimer's disease. An example is the Osaka mutation (Aβ1 …