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 …

Peptides and proteins have been found to possess an inherent tendency to convert from
their native functional states into intractable amyloid aggregates. This phenomenon is …

Chiral assemblies of plasmonic nanoparticles are known for strong circular dichroism but not
for high optical asymmetry, which is limited by the unfavorable combination of electrical and …

The number of biological therapeutic agents in the clinic and development pipeline has
increased dramatically over the last decade and the number will undoubtedly continue to …

In vitro, β-amyloid (Aβ) peptides form polymorphic fibrils, with molecular structures that
depend on growth conditions, plus various oligomeric and protofibrillar aggregates. Here …

Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the
quality of life of millions worldwide, with profound social and economic implications. Despite …

Our understanding of the molecular structures of amyloid fibrils that are associated with
neurodegenerative diseases, of mechanisms by which disease-associated peptides and …

Amyloid deposits consisting of fibrillar islet amyloid polypeptide (IAPP) in pancreatic islets
are associated with beta-cell loss and have been implicated in type 2 diabetes (T2D). Here …

The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose
homeostasis but aggregates to form islet amyloid in type‐2 diabetes. Islet amyloid formation …

Human islet amyloid polypeptide (hIAPP) functions as a glucose-regulating hormone but
deposits as amyloid fibrils in more than 90% of patients with type II diabetes (T2D). Here we …