Protein instability caused by exposure to external additives or severe stress may result in
different diseases. Of these diseases, many are triggered by protein misfolding and …

Many neurodegenerative diseases are rooted in the activities of amyloid-like proteins which
possess conformations that spread to healthy proteins. These include Alzheimer's disease …

Amyloid-β peptide (Aβ) forms metastable oligomers> 50 kDa, termed AβOs, that are more
effective than Aβ amyloid fibrils at triggering Alzheimer's disease-related processes such as …

Amyloid fibril formation of α-synuclein (αS) is associated with multiple neurodegenerative
diseases, including Parkinson's disease (PD). Growing evidence suggests that progression …

Amyloids share a common architecture but play disparate biological roles in processes
ranging from bacterial defense mechanisms to protein misfolding diseases. Their structures …

Amyloid‐β peptides (Aβ) assemble into both rigid amyloid fibrils and metastable oligomers
termed AβO or protofibrils. In Alzheimer's disease, Aβ fibrils constitute the core of senile …

Ultrasonication has been recently adopted in amyloid-fibril assays because of its ability to
accelerate fibril formation, being promising in the early stage diagnosis of amyloidoses in …

Formation of protein aggregates or fibrils entails the conversion of soluble native protein
monomers via multiple molecular states. No spectroscopic techniques have succeeded in …

Fibril formation of amyloid β (Aβ) peptides is one of the key molecular events connected to
Alzheimer's disease. The pathway of formation and mechanism of action of Aβ aggregates in …

A method is designed to quickly form protein hydrogels, based on the self-assembly of
highly concentrated lysozyme solutions in acidic conditions. Their properties can be easily …