The formation of nanoscale amyloid fibrils from normally soluble peptides and proteins is a
common form of self-assembly phenomenon that has fundamental connections with …

Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the growing
population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of …

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 …

Protein misfolding diseases are becoming increasingly prevalent, yet there are very few
effective pharmacological treatments. The onset and progression of these diseases is …

Amyloids are highly ordered protein/peptide aggregates associated with human diseases as
well as various native biological functions. Given the diverse range of physiochemical …

Amyloid formation reactions exhibit two classes of polymorphisms: the metastable
intermediates commonly observed during amyloid formation and the range of …

Amyloids are filamentous protein deposits ranging in size from nanometres to microns and
composed of aggregated peptide β-sheets formed from parallel or anti-parallel alignments of …

Amyloid fibrils are β-sheet-rich linear protein polymers that can be formed by a large variety
of different proteins. These assemblies have received much interest in recent decades, due …

Protein aggregation presents one of the key challenges in the development of protein
biotherapeutics. It affects not only product quality but also potentially impacts safety, as …

Human insulin has long been known to form amyloid fibrils under given conditions. The
molecular basis of insulin aggregation is relevant for modeling the amyloidogenesis …