Impact of Cu (ii) and Al (iii) on the Conformational Landscape of Amyloidβ 1-42
Metal ions have been found to play an important role in the formation of extracellular β-
amyloid plaques, a major hallmark of Alzheimer's disease. In the present study, the …
amyloid plaques, a major hallmark of Alzheimer's disease. In the present study, the …
Conformational transitions of the Amyloid‐β peptide upon copper (II) binding and pH changes
Amyloid‐β (Aβ) is a natively unfolded peptide found in all Alzheimer's disease patients as
the major component of fibrillar plaques, which are recognized as an important pathological …
the major component of fibrillar plaques, which are recognized as an important pathological …
Computational assessment of the impact of Cu(II) and Al(III) on β-amyloid42 fibrils: Binding sites, structural stability, and possible physiological implications
One of Alzheimer's disease major hallmarks is the aggregation of β-amyloid peptide, a
process in which metal ions play an important role. In the present work, an integrative …
process in which metal ions play an important role. In the present work, an integrative …
Impact of Cu(II) Binding on Structures and Dynamics of Aβ42 Monomer and Dimer: Molecular Dynamics Study
The classical force field, which is compatible with the Amber force field 99SB, has been
obtained for the interaction of Cu (II) with monomer and dimers of amyloid-β peptides using …
obtained for the interaction of Cu (II) with monomer and dimers of amyloid-β peptides using …
Computational Study of Amyloidβ42 Familial Mutations and Metal Interaction: Impact on Monomers and Aggregates Dynamical Behaviors
One of the main hallmarks of Alzheimer's Disease is the formation of β-amyloid plaques,
whose formation may be enhanced by metal binding or the appearance of familial …
whose formation may be enhanced by metal binding or the appearance of familial …
Molecular dynamics simulation of aluminium binding to amyloid-β and its effect on peptide structure
Multiple microsecond-length molecular dynamics simulations of complexes of Al (III) with
amyloid-β (Aβ) peptides of varying length are reported, employing a non-bonded model of Al …
amyloid-β (Aβ) peptides of varying length are reported, employing a non-bonded model of Al …
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 …
brains of Alzheimer's disease patients. These monomers and oligomers are largely …
Characterization of the polymorphic states of copper (II)‐bound Aβ (1–16) peptides by computational simulations
Understanding the polymorphic states of metal amyloid β (Aβ) interactions helps to elucidate
metal‐mediated events in the pathogenesis of Alzheimer's disease. Systematic …
metal‐mediated events in the pathogenesis of Alzheimer's disease. Systematic …
Molecular dynamics study of the beta amyloid peptide of Alzheimer's disease and its divalent copper complexes
DF Raffa, A Rauk - The Journal of Physical Chemistry B, 2007 - ACS Publications
The Aβ1− 42 monomer structure was assessed with a 790 ns molecular dynamics (MD)
simulation, and the results were compared with the NMR experiment on Aβ10− 35 and Aβ1 …
simulation, and the results were compared with the NMR experiment on Aβ10− 35 and Aβ1 …
Metal Binding to Amyloid-β1–42: A Ligand Field Molecular Dynamics Study
ST Mutter, M Turner, RJ Deeth… - ACS Chemical …, 2018 - ACS Publications
Ligand field molecular mechanics simulation has been used to model the interactions of
copper (II) and platinum (II) with the amyloid-β1–42 peptide monomer. Molecular dynamics …
copper (II) and platinum (II) with the amyloid-β1–42 peptide monomer. Molecular dynamics …