Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

Amyloid and amyloid-like fibrils are self-assembling protein nanostructures, of interest for
their robust material properties and inherent biological compatibility as well as their putative …

Amyloid fibrillation has been intensively studied because of its association with various
neurological disorders. While extensive time-dependent fibrillation experimental data are …

A central component of a number of degenerative diseases is the deposition of protein as
amyloid fibers. Self-assembly of amyloid occurs by a nucleation-dependent mechanism that …

Interest in amyloidogenesis has exploded in recent years, as scientists recognize the role of
amyloid protein aggregates in degenerative diseases such as Alzheimer's and Parkinson's …

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 …

At low pH insulin is highly prone to self-assembly into amyloid fibrils. The process has been
proposed to be affected by the existence of secondary nucleation pathways, in which …

Using the peptide hormone glucagon and Aβ (1–40) as model systems, we have sought to
elucidate the mechanisms by which fibrils grow and multiply. We here present real-time …

We here report an experimental study on the thermal aggregation process of concanavalin
A, a protein belonging to the legume lectins family. The aggregation process and the …

The traditional approach to investigating the partial unfolding and fibrillation of insulin, and
proteins at large, has involved use of the dyes 1-anilinonaphthalene-8-sulphonic acid (ANS) …