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 …

Effects of in vivo conditions on amyloid aggregation

MC Owen, D Gnutt, M Gao, SKTS Wärmländer… - Chemical Society …, 2019 - pubs.rsc.org
One of the grand challenges of biophysical chemistry is to understand the principles that
govern protein misfolding and aggregation, which is a highly complex process that is …

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 …

Alzheimer's disease: How metal ions define β-amyloid function

KP Kepp - Coordination Chemistry Reviews, 2017 - Elsevier
Alzheimer's disease is increasingly recognized to be linked to the function and status of
metal ions, and recently, the amyloid hypothesis has been strongly intertwined with the …

Transition metal ion interactions with disordered amyloid-β peptides in the pathogenesis of Alzheimer's disease: insights from computational chemistry studies

B Strodel, O Coskuner-Weber - Journal of chemical information …, 2019 - ACS Publications
Monomers and oligomers of the amyloid-β peptide aggregate to form the fibrils found in the
brains of Alzheimer's disease patients. These monomers and oligomers are largely …

Enhanced sampling and free energy calculations for protein simulations

Q Liao - Progress in molecular biology and translational …, 2020 - Elsevier
Molecular dynamics simulation is a powerful computational technique to study biomolecular
systems, which complements experiments by providing insights into the structural dynamics …

Aβ under stress: the effects of acidosis, Cu 2+-binding, and oxidation on amyloid β-peptide dimers

Q Liao, MC Owen, S Bali, B Barz… - Chemical communications, 2018 - pubs.rsc.org
In light of the high affinity of Cu2+ for Alzheimer's Aβ1–42 and its ability to subsequently
catalyze the formation of radicals, we examine the effects of Cu2+ binding, Aβ oxidation, and …

Compact fibril-like structure of amyloid β-peptide (1–42) monomers

B Barz, AK Buell, S Nath - Chemical communications, 2021 - pubs.rsc.org
Amyloid β (Aβ) monomers are the smallest assembly units, and play an important role in
most of the individual processes involved in amyloid fibril formation. An important question is …

Edaravone inhibits the conformational transition of amyloid-β42: Insights from molecular dynamics simulations

F Liu, Z Ma, J Sang, F Lu - Journal of Biomolecular Structure and …, 2020 - Taylor & Francis
Previous work has shown that edaravone inhibits fibrillogenesis of amyloid-β protein (Aβ).
However, the detailed mechanism by which edaravone inhibits the conformational transition …

Modular Protein Fibers with Outstanding High‐Strength and Acid‐Resistance Performance Mediated by Copper Ion Binding and Imine Networking

M Wang, Z Yang, B Jia, D Qin, Y Liu, F Wang… - Advanced …, 2024 - Wiley Online Library
Engineered protein fibers are promising biomaterials with diverse applications due to their
tunable protein structure and outstanding mechanical properties. However, it remains …