A variety of neurodegenerative diseases are associated with amyloid plaques, which begin
as soluble protein oligomers but develop into amyloid fibrils. Our incomplete understanding …

Molecular dynamics (MD) simulations have become popular in materials science,
biochemistry, biophysics and several other fields. Improvements in computational resources …

Nonfibrillar soluble oligomers, which are intermediates in the transition from monomers to
amyloid fibrils, may be the toxic species in Alzheimer's disease. To monitor the early events …

The progress toward understanding the molecular basis of Alzheimers's disease is strongly
connected to elucidating the early aggregation events of the amyloid-β (Aβ) peptide …

We investigated the effects of 17 widely used atomistic molecular mechanics force fields
(MMFFs) on the structures and kinetics of amyloid peptide assembly. To this end, we …

Alzheimer's disease is associated with the abnormal self-assembly of the amyloid-β (Aβ)
peptide into toxic β-rich aggregates. Experimental studies have shown that hydrophobic …

The role of water in promoting the formation of protofilaments (the basic building blocks of
amyloid fibrils) is investigated using fully atomic molecular dynamics simulations. Our model …

In the amyloid fibrils formed from long fragments of the amyloid β-protein (Aβ-protein), the
monomers are arranged in parallel and lie perpendicular to the fibril axis. The structure of …

It is known that oligomers of amyloid-β (Aβ) peptide are associated with Alzheimer's disease.
Aβ has two isoforms: Aβ40 and Aβ42. Although the difference between Aβ40 and Aβ42 is …

The aim of this work is to investigate the effects of molecular mechanics force fields on
amyloid peptide assembly. To this end, we performed extensive replica exchange molecular …