Molecular‐Dynamics Simulations for Amyloid β1–42 Monomer with D‐Aspartic Acid Residues Using Continuous Solvent

A Oda, K Kobayashi, O Takahashi - Chemistry & Biodiversity, 2010 - Wiley Online Library
Molecular‐dynamics simulations of amyloid‐β1–42 peptides including d‐aspartic acid
residues were performed, and their three‐dimensional structures were compared. The …

Computational study on the assembly of amyloid β-peptides in the hydrophobic environment

L Qu, S Fudo, K Matsuzaki, T Hoshino - … and Pharmaceutical Bulletin, 2019 - jstage.jst.go.jp
Fibrillated aggregation of amyloid β (Aβ) peptides is a potential factor causing toxic amyloid
deposition in neurodegenerative diseases. A toxic fibril formation of Aβ is known to be …

The effect of solvents on the conformations of Amyloid β-peptide (1–42) studied by molecular dynamics simulation

C Yang, J Li, Y Li, X Zhu - Journal of Molecular Structure: THEOCHEM, 2009 - Elsevier
Amyloid β-peptide (Aβ) is the major component of plaques found in the brains of Alzheimer's
patients. Among its two predominate forms− Aβ (1–40) and Aβ (1–42), the latter possesses …

General Dynamic Properties of Aβ12–36 Amyloid Peptide Involved in Alzheimer's Disease from Unfolding Simulation

S Suzuki, OV Galzitskaya, D Mitomo… - Journal of …, 2004 - academic.oup.com
To study the folding/unfolding properties of a β-amyloid peptide Aβ12–36 of Alzheimer's
disease, five molecular dynamics simulations of Aβ12–36 in explicit water were done at 450 …

Conformational transition of amyloid β-peptide

Y Xu, J Shen, X Luo, W Zhu, K Chen… - Proceedings of the …, 2005 - National Acad Sciences
The amyloid β-peptides (Aβs), containing 39–43 residues, are the key protein components
of amyloid deposits in Alzheimer's disease. To structurally characterize the dynamic …

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 …

Comparison of molecular dynamics simulation methods for amyloid β1–42 monomers containing d-aspartic acid residues for predicting retention times in …

A Oda, K Kobayashi, O Takahashi - Journal of Chromatography B, 2011 - Elsevier
Molecular dynamics simulations of amyloid β1–42 containing d-aspartic acid residues were
performed using several continuous solvent models to investigate the usefulness of …

Molecular Simulation of the amyloid β-peptide Aβ-(1-40) of Alzheimer's disease

PP Mager - Molecular Simulation, 1998 - Taylor & Francis
Abstract The amyloid Aβ (1–40) peptide of Alzheimer's disease was chosen as model
compound. This Aβ peptide is an intrinsically soluble peptide; the C-terminal amino acids …

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 …

All-atom molecular dynamics studies of the full-length β-amyloid peptides

E Luttmann, G Fels - Chemical physics, 2006 - Elsevier
β-Amyloid peptides are believed to play an essential role in Alzheimer's disease (AD), due
to their sedimentation in the form of β-amyloid aggregates in the brain of AD-patients, and …