Amyloid oligomers: A joint experimental/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis

PH Nguyen, A Ramamoorthy, BR Sahoo… - Chemical …, 2021‏ - ACS Publications
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Simulation studies of amyloidogenic polypeptides and their aggregates

IM Ilie, A Caflisch - Chemical reviews, 2019‏ - ACS Publications
Amyloids, fibrillar assembly of (poly) peptide chains, are associated with neurodegenerative
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …

Energy landscapes of protein aggregation and conformation switching in intrinsically disordered proteins

B Strodel - Journal of molecular biology, 2021‏ - Elsevier
The protein folding problem was apparently solved recently by the advent of a deep learning
method for protein structure prediction called AlphaFold. However, this program is not able …

Pathways of amyloid-β aggregation depend on oligomer shape

B Barz, Q Liao, B Strodel - Journal of the american chemical …, 2018‏ - ACS Publications
One of the main research topics related to Alzheimer's disease is the aggregation of the
amyloid-β peptide, which was shown to follow different pathways for the two major alloforms …

Structures of the intrinsically disordered Aβ, tau and α-synuclein proteins in aqueous solution from computer simulations

PH Nguyen, P Derreumaux - Biophysical Chemistry, 2020‏ - Elsevier
Intrinsically disordered proteins (IDPs) play many biological roles in the human proteome
ranging from vesicular transport, signal transduction to neurodegenerative diseases. The Aβ …

Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane

H Fatafta, M Khaled, MC Owen… - Proceedings of the …, 2021‏ - pnas.org
Mounting evidence suggests that the neuronal cell membrane is the main site of oligomer-
mediated neuronal toxicity of amyloid-β peptides in Alzheimer's disease. To gain a detailed …

Key residue for aggregation of Amyloid-β peptides

SG Itoh, M Yagi-Utsumi, K Kato… - ACS Chemical …, 2022‏ - ACS Publications
It is known that oligomers of amyloid-β (Aβ) peptide are associated with Alzheimer's disease.
Aβ has two isoforms: Aβ40 and Aβ42. Although the difference between Aβ40 and Aβ42 is …

High-resolution structures of the amyloid-β 1–42 dimers from the comparison of four atomistic force fields

VH Man, PH Nguyen… - The Journal of Physical …, 2017‏ - ACS Publications
The dimer of the amyloid-β peptide Aβ of 42 residues is the smallest toxic species in
Alzheimer's disease, but its equilibrium structures are unknown. Here we determined the …

Advances in the simulation of protein aggregation at the atomistic scale

M Carballo-Pacheco, B Strodel - The journal of physical chemistry …, 2016‏ - ACS Publications
Protein aggregation into highly structured amyloid fibrils is associated with various diseases
including Alzheimer's disease, Parkinson's disease, and type II diabetes. Amyloids can also …

An account of amyloid oligomers: facts and figures obtained from experiments and simulations

L Nagel‐Steger, MC Owen, B Strodel - ChemBioChem, 2016‏ - Wiley Online Library
The deposition of amyloid in brain tissue in the context of neurodegenerative diseases
involves the formation of intermediate species—termed oligomers—of lower molecular mass …