One of the grand challenges of biophysical chemistry is to understand the principles that
govern protein misfolding and aggregation, which is a highly complex process that is …

Amyloidogenic diseases are characterised by the formation of amyloid aggregates inside or
outside the cell. Amyloid-associated human diseases include Alzheimer's disease …

Highlights•A range of functionally and structurally unrelated proteins form amyloid.•Toxic
intermediates remain elusive, making their targeting a significant challenge.•Design and …

The conversion of proteins from their soluble states into well-organized fibrillar aggregates is
associated with a wide range of pathological conditions, including neurodegenerative …

Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Protein and peptide aggregation raises keen interest due to their involvement in number of
pathological conditions ranging from neurodegenerative disorders to systemic amyloidosis …

Inhibition of amyloid β peptide (Aβ) aggregation is an important goal due to the connection
of this process with Alzheimer's disease. Traditionally, inhibitors were developed with an aim …

Aggregation of the amyloid-β (Aβ) peptide is strongly correlated with Alzheimer's disease
(AD). Recent research has improved our understanding of the kinetics of amyloid fibril …

Protein aggregation underlies an array of human diseases, yet only one small-molecule
therapeutic targeting this process has been successfully developed to date. Here, we …

Understanding the mechanisms underlying protein misfolding and aggregation has become
a central issue in biology and medicine. Compelling evidence show that the formation of …