Role of water molecules and helix structure stabilization in the laser-induced disruption of amyloid fibrils observed by nonequilibrium molecular dynamics simulations

H Okumura, SG Itoh, K Nakamura… - The Journal of Physical …, 2021 - ACS Publications
Water plays a crucial role in the formation and destruction of biomolecular structures. The
mechanism for destroying biomolecular structures was thought to be an active breaking of …

Effects of a hydrophilic/hydrophobic interface on amyloid-β peptides studied by molecular dynamics simulations and NMR experiments

SG Itoh, M Yagi-Utsumi, K Kato… - The Journal of Physical …, 2018 - ACS Publications
Oligomer formation of amyloid-β peptides (Aβ) is accelerated at a hydrophilic/hydrophobic
interface. However, details of the acceleration mechanism have not been elucidated. To …

Structural and fluctuational difference between two ends of Aβ amyloid fibril: MD simulations predict only one end has open conformations

H Okumura, SG Itoh - Scientific reports, 2016 - nature.com
A β amyloid fibrils, which are related to Alzheimer's disease, have a cross-β structure
consisting of two β-sheets: β 1 and β 2. The A β peptides are thought to be serially arranged …

Multistep conformation selection in amyloid assembly

MC Hsieh, C Liang, AK Mehta, DG Lynn… - Journal of the …, 2017 - ACS Publications
Defining pathways for amyloid assembly could impact therapeutic strategies for as many as
50 disease states. Here we show that amyloid assembly is subject to different forces …

Curcumin Binds to Aβ1–40 Peptides and Fibrils Stronger Than Ibuprofen and Naproxen

ST Ngo, MS Li - The Journal of Physical Chemistry B, 2012 - ACS Publications
Binding of curcumin, naproxen, and ibuprofen to Aβ1–40 peptide and its fibrils is studied by
docking method and all-atom molecular dynamics simulations. The Gromos96 43a1 force …

The molecular processes underpinning prion-like spreading and seed amplification in protein aggregation

G Meisl, TPJ Knowles, D Klenerman - Current opinion in neurobiology, 2020 - Elsevier
Highlights•Kinetics yield mechanism and rates of aggregation of tau, PrP, Aβ and α-syn in
vitro.•Animal models provide evidence for differences and similarities in mechanisms in …

Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragment

DW Li, S Mohanty, A Irbäck, S Huo - PLoS computational biology, 2008 - journals.plos.org
Small oligomers formed early in the process of amyloid fibril formation may be the major
toxic species in Alzheimer's disease. We investigate the early stages of amyloid aggregation …

Looking at the disordered proteins through the computational microscope

P Das, S Matysiak, J Mittal - ACS central science, 2018 - ACS Publications
Intrinsically disordered proteins (IDPs) have attracted wide interest over the past decade due
to their surprising prevalence in the proteome and versatile roles in cell physiology and …

Thermodynamics and dynamics of amyloid peptide oligomerization are sequence dependent

Y Lu, P Derreumaux, Z Guo… - Proteins: Structure …, 2009 - Wiley Online Library
Aggregation of the full‐length amyloid‐β (Aβ) and β2‐microglobulin (β2m) proteins is
associated with Alzheimer's disease and dialysis‐related amyloidosis, respectively. This …

Mechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field

A Rojas, A Liwo, D Browne, HA Scheraga - Journal of Molecular Biology, 2010 - Elsevier
The growth mechanism of β-amyloid (Aβ) peptide fibrils was studied by a physics-based
coarse-grained united-residue model and molecular dynamics (MD) simulations. To identify …