Molecular dynamics simulations in explicit water were carried out for two stacks, each
composed of six 10‐strand antiparallel β‐sheets for two peptides corresponding to the …

Molecular dynamics (MD) simulations were carried out for two‐strand and ten‐strand β‐
sheets constructed from two peptides corresponding to the diverging turn of two homologous …

The amyloid aggregation of human islet amyloid polypeptide (hIAPP) is associated with
pancreatic β-cell death in type 2 diabetes. The S20G substitution of hIAPP (hIAPP (S20G)) …

The aggregation observed in protein conformational diseases is the outcome of significant
new β‐sheet structure not present in the native state. Peptide model systems have been …

Our task was to determine the most stable packing of peptides in β-layers to construct an
oligomer structure for fibril growth. The β-layers consisting of eight short peptides with the …

Alzheimer's disease (AD) pathogenesis is associated with formation of amyloid fibrils
caused by polymerization of the amyloid β-peptide (Aβ), which is a process that requires …

Experiments suggested that the fibrillation of the 11–25 fragment (hIAPP (11–25)) of human
islet amyloid polypeptide (hIAPP or amylin) involves the formation of transient α-helical …

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 …

Molecular‐dynamics simulations of amyloid‐β1–42 peptides including d‐aspartic acid
residues were performed, and their three‐dimensional structures were compared. The …

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 …