Effect of Taiwan mutation (D7H) on structures of amyloid-β peptides: replica exchange molecular dynamics study

PM Truong, MH Viet, PH Nguyen… - The Journal of Physical …, 2014 - ACS Publications
Recent experiments have shown that the Taiwan mutation (D7H) slows the fibril formation of
amyloid peptides Aβ40 and Aβ42. Motivated by this finding, we have studied the influence of …

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 …

Molecular dynamics studies of hexamers of amyloid‐β peptide (16–35) and its mutants: Influence of charge states on amyloid formation

W Han, YD Wu - Proteins: Structure, Function, and …, 2007 - Wiley Online Library
To study the early stage of amyloid‐β peptide (Aβ) aggregation, hexamers of the wild‐type
(WT) Aβ16–35 and its mutants with amyloid‐like conformations have been studied by …

Side chain interactions can impede amyloid fibril growth: replica exchange simulations of Aβ peptide mutant

T Takeda, DK Klimov - The Journal of Physical Chemistry B, 2009 - ACS Publications
Using replica exchange molecular dynamics, we study the effect of Asp23Tyr mutation on
Aβ10− 40 fibril growth. The effect of this mutation is revealed through the computation of free …

Amyloid peptide Aβ40 inhibits aggregation of Aβ42: Evidence from molecular dynamics simulations

MH Viet, MS Li - The Journal of Chemical Physics, 2012 - pubs.aip.org
Effects of amyloid beta (Aβ) peptide Aβ 40 on secondary structures of Aβ 42 are studied by
all-atom simulations using the GROMOS96 43a1 force field with explicit water. It is shown …

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 …

Stable conformation of full-length amyloid-β (1–42) monomer in water: Replica exchange molecular dynamics and ab initio molecular orbital simulations

A Okamoto, A Yano, K Nomura, S Higai… - Chemical Physics Letters, 2013 - Elsevier
Aggregation of amyloid β-proteins (Aβ) plays a key role in the mechanism of molecular
pathogenesis of Alzheimer's disease (AD). It is known that full-length Aβ (1–42) is more …

Influence of preformed asp23− lys28 salt bridge on the conformational fluctuations of monomers and dimers of Aβ peptides with implications for rates of fibril formation

G Reddy, JE Straub, D Thirumalai - The journal of physical …, 2009 - ACS Publications
Recent experiments have shown that the congener Aβ1− 40 [D23− K28], in which the side
chains of charged residues Asp23 and Lys28 are linked by a lactam bridge, forms amyloid …

Aggregation rate of amyloid beta peptide is controlled by beta-content in monomeric state

TTM Thu, NT Co, LA Tu, MS Li - The Journal of chemical physics, 2019 - pubs.aip.org
Understanding the key factors that govern the rate of protein aggregation is of immense
interest since protein aggregation is associated with a number of neurodegenerative …

Effects of different force fields and temperatures on the Structural character of abeta (12–28) peptide in aqueous solution

Z Cao, L Liu, L Zhao, J Wang - International Journal of Molecular …, 2011 - mdpi.com
The aim of this work is to investigate the effects of different force fields and temperatures on
the structural character of Aβ (12–28) peptide in aqueous solution. Moreover, the structural …