Molecular dynamics simulations to investigate the aggregation behaviors of the aß (17–42) oligomers

JH Zhao, HL Liu, YF Liu, HY Lin, HW Fang… - Journal of …, 2009 - Taylor & Francis
The amyloid β-peptides (Aßs) are the main protein components of amyloid deposits in
Alzheimer's disease (AD). Detailed knowledge of the structure and assembly dynamics of Aß …

Novel Disassembly Mechanisms of Sigmoid Aβ42 Protofibrils by Introduced Neutral and Charged Drug Molecules

X Xing, C Liu, A Ali, B Kang, P Li… - ACS Chemical …, 2019 - ACS Publications
Alzheimer's disease (AD) is characterized by fibrillar deposits of amyloid-β (Aβ) peptides
and neurofibrillary tangles of Tau proteins. Aβ peptides are composed of 37–49 residues …

Mechanistic kinetic model reveals how amyloidogenic hydrophobic patches facilitate the amyloid-β fibril elongation

H Xie, A Rojas, GG Maisuradze… - ACS chemical …, 2022 - ACS Publications
Abnormal aggregation of amyloid β (Aβ) peptides into fibrils plays a critical role in the
development of Alzheimer's disease. A two-stage “dock-lock” model has been proposed for …

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 …

X-ray Crystallography Reveals Parallel and Antiparallel β-Sheet Dimers of a β-Hairpin Derived from Aβ16–36 that Assemble to Form Different Tetramers

AG Kreutzer, TD Samdin, G Guaglianone… - ACS chemical …, 2020 - ACS Publications
High-resolution structures of oligomers formed by the β-amyloid peptide, Aβ, are important
for understanding the molecular basis of Alzheimer's disease. Dimers of Aβ are linked to the …

[HTML][HTML] Large fatty acid-derived Aβ42 oligomers form ring-like assemblies

W Xi, DN Dean, KA Stockmal, SE Morgan… - The Journal of …, 2019 - pubs.aip.org
As the primary toxic species in the etiology of Alzheimer disease (AD) are low molecular
weight oligomers of Aβ, it is crucial to understand the structure of Aβ oligomers for gaining …

Pyroglutamate-modified amyloid β (3–42) monomer has more β-sheet content than the amyloid β (1–42) monomer

S Nath, AK Buell, B Barz - Physical Chemistry Chemical Physics, 2023 - pubs.rsc.org
The aggregation of the amyloid β (Aβ) peptide is a major hallmark of Alzheimer's disease.
This peptide can aggregate into oligomers, proto-fibrils and mature fibrils, which eventually …

Conversion between parallel and antiparallel β-sheets in wild-type and Iowa mutant Aβ40 fibrils

W Xi, UHE Hansmann - The Journal of Chemical Physics, 2018 - pubs.aip.org
Using a variant of Hamilton-replica-exchange, we study for wild type and Iowa mutant Aβ 40
the conversion between fibrils with antiparallel β-sheets and such with parallel β-sheets. We …

[HTML][HTML] New insights into the mechanism of Alzheimer amyloid-β fibrillogenesis inhibition by N-methylated peptides

P Soto, MA Griffin, JE Shea - Biophysical Journal, 2007 - cell.com
Alzheimer's disease is a debilitating neurodegenerative disorder associated with the
abnormal self-assembly of amyloid-β (Aβ) peptides into fibrillar species. N-methylated …

9, 10‐Anthraquinone hinders β‐aggregation: How does a small molecule interfere with Aβ‐peptide amyloid fibrillation?

M Convertino, R Pellarin, M Catto, A Carotti… - Protein …, 2009 - Wiley Online Library
Amyloid aggregation is linked to a number of neurodegenerative syndromes, the most
prevalent one being Alzheimer's disease. In this pathology, the β‐amyloid peptides (Aβ) …