Metastable oligomeric and protofibrillar forms of amyloidogenic proteins have been
implicated as on-pathway assembly intermediates in amyloid formation and as the major …

The abnormal aggregation of β-amyloid (Aβ) peptides in the brain is a major pathological
hallmark of Alzheimer's disease (AD). The suppression (or alteration) of Aβ aggregation is …

Insoluble amyloid formation by islet amyloid polypeptide (IAPP) in the islets of Langerhans
of the pancreas is a major pathophysiological feature of noninsulin dependent diabetes …

Escherichia coli is one of the most widely used hosts for the production of recombinant
proteins. However, very often the target protein accumulates into insoluble aggregates in a …

Pancreatic amyloid deposits, composed of the 37 amino acid residue peptide amylin,
represent an integral part of type 2 diabetes mellitus pathology. Human amylin (hA) forms …

The presence of fibrillar protein deposits (amyloid) of human islet amyloid polypeptide
(hIAPP) in the pancreatic islets of Langerhans is thought to be related to death of the insulin …

Evidence is growing at an increasing pace that amyloid fibers are not just the result of
aberrant protein folding associated with neurodegenerative diseases, but are widespread in …

Because of their commanding properties, ultrashort and short peptides are gaining
significance as viable candidates for molecular self-assembly, which is a naturally inspired …

Alzheimer's disease (AD) is the most common form of dementia. The development of assay
technologies able to diagnose early-stage AD is important. Blood tests to detect biomarkers …

Amylin is primarily responsible for classifying type II diabetes as an amyloid (protein
misfolding) disease as it has great potential to aggregate into toxic nanoparticles, thereby …