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 …

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 …

Structural interconversion in Alzheimer's Amyloid-β (16–35) peptide in an aqueous solution

NA Alves, RB Frigori - The Journal of Physical Chemistry B, 2018 - ACS Publications
Structural properties of Aβ (16–35) fragment are investigated as a model for the amyloid-β
peptide excluding its coil-inducing terminals. Our replica-exchange molecular dynamics …

The structure of the Alzheimer amyloid β 10-35 peptide probed through replica-exchange molecular dynamics simulations in explicit solvent

A Baumketner, JE Shea - Journal of molecular biology, 2007 - Elsevier
The conformational states sampled by the Alzheimer amyloid β (10-35)(Aβ 10-35) peptide
were probed using replica-exchange molecular dynamics (REMD) simulations in explicit …

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 …

Why Is the C-terminus of Aβ (1− 42) More Unfolded than That of Aβ (1− 40)? Clues from Hydrophobic Interaction

L Shen, HF Ji, HY Zhang - The Journal of Physical Chemistry B, 2008 - ACS Publications
Aβ (1− 40) and Aβ (1− 42) are the main forms of amyloid β (Aβ) peptides in the brain of
Alzheimer's patients; however, the latter possesses much stronger aggregation and …

Molecular dynamics simulation study on conformational behavior of Aβ (1–40) and Aβ (1–42) in water and methanol

C Yang, X Zhu, J Li, K Chen - Journal of Molecular Structure: THEOCHEM, 2009 - Elsevier
Aβ (1–40) and Aβ (1–42) are the two predominant forms of amyloid β-peptide (Aβ) in the
plaques found in the brains of Alzheimer's patients. They possess identical amino acid …

Simulation study on the disordered state of an Alzheimer's β amyloid peptide Aβ (12–36) in water consisting of random‐structural, β‐structural, and helical clusters

J Ikebe, N Kamiya, JI Ito, H Shindo, J Higo - Protein science, 2007 - Wiley Online Library
The monomeric Alzheimer's β amyloid peptide, Aβ, is known to adopt a disordered state in
water at room temperature, and a circular dichroism (CD) spectroscopy experiment has …

Molecular dynamics simulation of the conformational transition of amyloid peptide 42 inhibited by trehalose

FF LIU, XY DONG, Y SUN - Acta Physico-Chimica Sinica, 2010 - ingentaconnect.com
The molecular mechanism of the conformational transition of amyloid peptide 42 (Aβ42)
inhibited by trehalose was studied using molecular dynamics simulation. It is confirmed that …