Effect of familial mutations on the interconversion of α-Helix to β-sheet structures in an amyloid-forming peptide: insight from umbrella sampling simulations
Understanding the initial events of aggregation of amyloid β monomers to form β-sheet rich
fibrils is useful for the development of therapeutics for Alzheimer's disease. In this context …
fibrils is useful for the development of therapeutics for Alzheimer's disease. In this context …
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 …
Assembly of amyloid β peptides in the presence of fibril seeds: One-pot coarse-grained molecular dynamics simulations
The identification of a secondary nucleation pathway in the early aggregation of amyloid
peptides suggests that the generation of toxic oligomers involves both monomers and …
peptides suggests that the generation of toxic oligomers involves both monomers and …
Compact fibril-like structure of amyloid β-peptide (1–42) monomers
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 …
most of the individual processes involved in amyloid fibril formation. An important question is …
Side chain interactions can impede amyloid fibril growth: replica exchange simulations of Aβ peptide mutant
Using replica exchange molecular dynamics, we study the effect of Asp23Tyr mutation on
Aβ10− 40 fibril growth. The effect of this mutation is revealed through the computation of free …
Aβ10− 40 fibril growth. The effect of this mutation is revealed through the computation of free …
Polymorphic structures of Alzheimer's β-amyloid globulomers
Background Misfolding and self-assembly of Amyloid-β (Aβ) peptides into amyloid fibrils is
pathologically linked to the development of Alzheimer's disease. Polymorphic Aβ structures …
pathologically linked to the development of Alzheimer's disease. Polymorphic Aβ structures …
[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 …
Emergence of barrel motif in amyloid-β trimer: a computational study
Amyloid-β (Aβ) peptides form assemblies that are pathological hallmarks of Alzheimer's
disease. Aβ oligomers are soluble, mobile, and toxic forms of the peptide that act in the …
disease. Aβ oligomers are soluble, mobile, and toxic forms of the peptide that act in the …
Mechanistic insight into E22Q-mutation-induced antiparallel-to-parallel β-sheet transition of Aβ 16− 22 fibrils: an all-atom simulation study
Alzheimer's disease is associated with the abnormal self-assembly of amyloid-β (Aβ)
peptide into toxic oligomers and fibrils. Recent experiments reported that Aβ16− 22 …
peptide into toxic oligomers and fibrils. Recent experiments reported that Aβ16− 22 …
[PDF][PDF] Unlocking the atomic-level details of amyloid fibril growth through advanced biomolecular simulations
NV Buchete - Biophysical journal, 2012 - cell.com
Molecular fibrils formed by aggregated amyloid peptides of various lengths and sequences
are common pathological fingerprints of a large range of amyloid-related diseases, from type …
are common pathological fingerprints of a large range of amyloid-related diseases, from type …