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 …
Self-assembly of the full-length amyloid Aβ42 protein in dimers
The self-assembly of amyloid (Aβ) proteins into nano-aggregates is a hallmark of
Alzheimer's disease (AD) development, yet the mechanism of how disordered monomers …
Alzheimer's disease (AD) development, yet the mechanism of how disordered monomers …
Spontaneous self-assembly of amyloid β (1–40) into dimers
The self-assembly and fibrillation of amyloid β (Aβ) proteins is the neuropathological
hallmark of Alzheimer's disease. However, the molecular mechanism of how disordered …
hallmark of Alzheimer's disease. However, the molecular mechanism of how disordered …
[PDF][PDF] Role of β-hairpin formation in aggregation: the self-assembly of the amyloid-β (25–35) peptide
L Larini, JE Shea - Biophysical journal, 2012 - cell.com
Abstract The amyloid-β (25–35) peptide plays a key role in the etiology of Alzheimer's
disease due to its extreme toxicity even in the absence of aging. Because of its high …
disease due to its extreme toxicity even in the absence of aging. Because of its high …
Assembly of Alzheimer's Aβ peptide into nanostructured amyloid fibrils
I Morgado, M Fändrich - Current opinion in colloid & interface science, 2011 - Elsevier
The self-assembly of β-amyloid (Aβ) peptide into highly ordered amyloid fibril structures
represents one of the pathological hallmarks of Alzheimer's disease. This process leads to …
represents one of the pathological hallmarks of Alzheimer's disease. This process leads to …
[PDF][PDF] Molecular dynamics simulations of amyloid β-peptide (1-42): tetramer formation and membrane interactions
The aggregation cascade and peptide-membrane interactions of the amyloid β-peptide (Aβ)
have been implicated as toxic events in the development and progression of Alzheimer's …
have been implicated as toxic events in the development and progression of Alzheimer's …
Computer Simulation Studies of Aβ37–42 Aggregation Thermodynamics and Kinetics in Water and Salt Solution
YI Yang, YQ Gao - The Journal of Physical Chemistry B, 2015 - ACS Publications
In vivo self-assembly of proteins into aggregates known as amyloids is related to many
diseases. Although a large number of studies have been performed on the formation of …
diseases. Although a large number of studies have been performed on the formation of …
Structure of ring-shaped Aβ42 oligomers determined by conformational selection
The oligomerization of amyloid beta (Aβ) peptides into soluble non-fibrillar species plays a
critical role in the pathogenesis of Alzheimer's disease. However, it has been challenging to …
critical role in the pathogenesis of Alzheimer's disease. However, it has been challenging to …
[PDF][PDF] Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer
The aggregation of amyloid beta (Aβ) peptides plays an important role in the development of
Alzheimer's disease. Despite extensive effort, it has been difficult to characterize the …
Alzheimer's disease. Despite extensive effort, it has been difficult to characterize the …
[PDF][PDF] Role of electrostatic interactions in amyloid β-protein (Aβ) oligomer formation: a discrete molecular dynamics study
Pathological folding and oligomer formation of the amyloid β-protein (Aβ) are widely
perceived as central to Alzheimer's disease. Experimental approaches to study Aβ self …
perceived as central to Alzheimer's disease. Experimental approaches to study Aβ self …