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 …

[HTML][HTML] 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 …

Early aggregation mechanism of Aβ16− 22 revealed by Markov state models

MU Rahman, K Song, LT Da, HF Chen - International Journal of Biological …, 2022 - Elsevier
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 …

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 …

Dissecting the molecular mechanisms of the co-aggregation of Aβ40 and Aβ42 peptides: a REMD simulation study

X Li, Z Yang, Y Chen, S Zhang, G Wei… - The Journal of Physical …, 2023 - ACS Publications
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 …

[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 …

Role of the region 23-28 in Aβ fibril formation: insights from simulations of the monomers and dimers of Alzheimer's peptides Aβ40 and Aβ42

A Melquiond, X Dong, N Mousseau… - Current Alzheimer …, 2008 - ingentaconnect.com
Self-assembly of the 40/42 amino acid Aβ peptide is a key player in Alzheimer's disease.
Aβ40 is the most prevalent species, while Aβ42 is the most toxic. It has been suggested that …

Tuning self-assembled morphology of the Aβ (16–22) peptide by substitution of phenylalanine residues

J Wang, K Tao, P Zhou, E Pambou, Z Li, H Xu… - Colloids and Surfaces B …, 2016 - Elsevier
The effects of the two phenylalanine (Phe) residues in the blocked Aβ (16–22) peptide on its
self-assembly have been investigated by replacing both of them with two cyclohexylalanines …

Structural insights into the co-aggregation of Aβ and tau amyloid core peptides: revealing potential pathological heterooligomers by simulations

X Li, Y Chen, Z Yang, S Zhang, G Wei… - International Journal of …, 2024 - Elsevier
The self-aggregation of amyloid-β (Aβ) and tau proteins are closely implicated in Alzheimer's
disease (AD). Recent evidence indicates that Aβ and tau proteins can cross-interact to form …

Metastable alpha‐rich and beta‐rich conformations of small Aβ42 peptide oligomers

PH Nguyen, F Sterpone… - … : Structure, Function, and …, 2023 - Wiley Online Library
Probing the structures of amyloid‐β (Aβ) peptides in the early steps of aggregation is
extremely difficult experimentally and computationally. Yet, this knowledge is extremely …