A great deal must still be learnt on the structural features of amyloid assemblies, particularly
prefibrillar aggregates, and the relationship of the latter with amyloid cytotoxicity. Presently, it …

Amyloid diseases display the presence, in targeted tissues and organs, of fibrillar deposits of
specific peptides or proteins. Increasing efforts are presently spent in investigating the …

Nanoparticles present enormous surface areas and are found to enhance the rate of protein
fibrillation by decreasing the lag time for nucleation. Protein fibrillation is involved in many …

Systemic light chain (LC) amyloidosis (AL) is a disease where organs are damaged by an
overload of a misfolded patient-specific antibody-derived LC, secreted by an abnormal B cell …

Aβ fibrils (or Abeta nanowires, NWs) have been implicated in many neurodegenerative
disorders such as Alzheimer disease (AD).[1] Both soluble oligomers and mature fibrils from …

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

Numerous studies of amyloid assembly have indicated that partially folded protein species
are responsible for initiating aggregation. Despite their importance, the structural and …

Amyloid is an abnormal extracellular fibrillar protein deposit in the tissues. In humans, more
than 25 different proteins can adopt a fibrillar conformation in vivo that results in the …

Peptide amyloid aggregation is a hallmark of several human pathologies termed amyloid
diseases. We have investigated the effect of electrostatically stabilized magnetic …

Amyloid cytotoxicity, structure and polymorphisms are themes of increasing importance.
Present knowledge considers any peptide/protein able to undergo misfolding and …