A major feature of Alzheimer's disease (AD) pathology is the plaque composed of
aggregated amyloid-β (Aβ) peptide. Although these plaques may have harmful properties …

Amyloids can have normal biological functions. 1r3 However, amyloidogenic proteins can
also form unwanted oligomeric or polymeric aggregates when disturbed from their native …

The aberrant assembly of peptides and proteins into fibrillar aggregates proceeds through
oligomeric intermediates that are thought to be the primary pathogenic species in many …

Amyloid-beta (Aβ) aggregates are the main constituent of senile plaques, the histological
hallmark of Alzheimer's disease. Aβ molecules form β-sheet containing structures that …

Heteromultivalency, which involves the simultaneous interactions of more than one type of
ligand with more than one type of receptor, is ubiquitous in living systems and provides a …

Amyloids are pathogenic hallmarks in many neurodegenerative diseases such as amyloid‐β
(Aβ) fibrils in Alzheimer's disease (AD). Here, the effect of gold nanoparticles (AuNPs) on …

Protein misfolding and aggregation cause serious degenerative conditions such as
Alzheimer's, Parkinson, and prion diseases. Damage to membranes is thought to be one of …

The dynamics, energies, and structures governing protein folding are critical to biological
function. Amyloidoses are a class of disease defined, in part, by the misfolding and …

Since the reformulation of the amyloid cascade hypothesis to focus on oligomeric
aggregates of amyloid beta as the prime toxic species causing Alzheimer's disease, many …

A combination of hydrophobic and electrostatic interactions is important in initiating the
aberrant self-assembly process that leads to formation of toxic oligomers and aggregates by …