Structure, orientation, and surface interaction of Alzheimer amyloid-β peptides on the graphite
The misfolding and aggregation of amyloid-β (Aβ) peptides into amyloid fibrils in solution
and on the cell membrane has been linked to the pathogenesis of Alzheimer's disease …
and on the cell membrane has been linked to the pathogenesis of Alzheimer's disease …
Alzheimer Aβ1−42 Monomer Adsorbed on the Self-Assembled Monolayers
Amyloid-β (Aβ) peptide aggregation on the cell membranes is a key pathological event
responsible for neuron cell death in Alzheimer's disease (AD). We present a collection of …
responsible for neuron cell death in Alzheimer's disease (AD). We present a collection of …
In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: New insights into mechanism of β-sheet formation
T Kowalewski, DM Holtzman - Proceedings of the National …, 1999 - National Acad Sciences
We have applied in situ atomic force microscopy to directly observe the aggregation of
Alzheimer's β-amyloid peptide (Aβ) in contact with two model solid surfaces: hydrophilic …
Alzheimer's β-amyloid peptide (Aβ) in contact with two model solid surfaces: hydrophilic …
Fibrillation-prone conformations of the amyloid-β-42 peptide at the gold/water interface
Proteins in the proximity of inorganic surfaces and nanoparticles may undergo profound
adjustments that trigger biomedically relevant processes, such as protein fibrillation. The …
adjustments that trigger biomedically relevant processes, such as protein fibrillation. The …
A novel pathway for amyloids self-assembly in aggregates at nanomolar concentration mediated by the interaction with surfaces
A limitation of the amyloid hypothesis in explaining the development of neurodegenerative
diseases is that the level of amyloidogenic polypeptide in vivo is below the critical …
diseases is that the level of amyloidogenic polypeptide in vivo is below the critical …
Promotion and inhibition of amyloid-β peptide aggregation: Molecular dynamics studies
Aggregates of amyloid-β (Aβ) peptides are known to be related to Alzheimer's disease. Their
aggregation is enhanced at hydrophilic–hydrophobic interfaces, such as a cell membrane …
aggregation is enhanced at hydrophilic–hydrophobic interfaces, such as a cell membrane …
Comparative molecular dynamics study of Aβ adsorption on the self-assembled monolayers
The adsorption and aggregation of the amyloid-β (Aβ) peptides on the cell membrane plays
a causal role in the pathogenesis of Alzheimer's disease. Here, we report all-atom molecular …
a causal role in the pathogenesis of Alzheimer's disease. Here, we report all-atom molecular …
Structural, morphological, and kinetic studies of β-amyloid peptide aggregation on self-assembled monolayers
Q Wang, N Shah, J Zhao, C Wang, C Zhao… - Physical Chemistry …, 2011 - pubs.rsc.org
The misfolding and aggregation of β-amyloid peptides (Aβ) into amyloid fibrils, a process
that has been pathologically linked to the onset of Alzheimer's disease, is dependent on the …
that has been pathologically linked to the onset of Alzheimer's disease, is dependent on the …
Polymorphism of amyloid β peptide in different environments: implications for membrane insertion and pore formation
Amyloid-β (Aβ) peptides are thought to be involved in neurodegenerative diseases such as
Alzheimer's disease and Down's syndrome. They form a large number of polymorphic …
Alzheimer's disease and Down's syndrome. They form a large number of polymorphic …
Molecular dynamics simulations of amyloid-β (16–22) peptide aggregation at air–water interfaces
Oligomers of amyloid-β (Aβ) peptides are known to be related to Alzheimer's disease, and
their formation is accelerated at hydrophilic–hydrophobic interfaces, such as the cell …
their formation is accelerated at hydrophilic–hydrophobic interfaces, such as the cell …