Alzheimer's disease is the most fatal neurodegenerative disorder characterized by the
aggregation and deposition of Amyloid β (Aβ) oligomers in the brain of patients. Two …

The amyloid β-peptides (Aβs), containing 39–43 residues, are the key protein components
of amyloid deposits in Alzheimer's disease. To structurally characterize the dynamic …

The influence of charge and aromatic stacking interactions on the self-assembly of a series
of four model amyloid peptides has been examined. The four model peptides are based on …

The amyloid β-protein (Aβ), which is present predominately as a 40-or 42-residue peptide, is
postulated to play a seminal role in the pathogenesis of Alzheimer's disease (AD). Folding of …

Amyloid-β (Aβ) peptides exhibit many distinct structural morphology at the early aggregate
stage, some of which are biological relevant to the pathogenesis of Alzheimer's disease …

The aggregation of the amyloid β (Aβ) peptide is a major hallmark of Alzheimer's disease.
This peptide can aggregate into oligomers, proto-fibrils and mature fibrils, which eventually …

Using replica exchange molecular dynamics (REMD) and united atom implicit solvent model
we examine the role of backbone hydrogen bonds (HBs) in Aβ aggregation. The importance …

Human islet amyloid polypeptide (hIAPP or amylin) is a causative agent in pancreatic
amyloid deposits found in patients with type 2 diabetes. The aggregation of full-length …

In this paper, all-atom molecular dynamics simulations in explicit solvent are used to
investigate the structural and dynamical determinants of the α-helical to β-hairpin …

The development of specific agents against amyloidoses requires an understanding of the
conformational distribution of fibrillogenic peptides at a microscopic level. Here, I present …