Protein self-assembly and formation of amyloid fibers is an early event of numerous human
diseases. Continuous aggregation of amyloid fibers in vitro produces biogels, which led us …

Amyloid fibers are associated with disease but have little chemical reactivity. We
investigated the formation and structure of amyloids to identify potential mechanisms for their …

Aβ (1–40) is one of the main components of the fibrils found in amyloid plaques, a hallmark
of brains affected by Alzheimer's disease. It is known that prior to the formation of amyloid …

Many chronic degenerative diseases result from aggregation of misfolded polypeptides to
form amyloids. Many amyloidogenic polypeptides are surfactants and their assembly can be …

Accumulation of aggregated amyloid-β peptide (Aβ) in the brain is a pathological hallmark of
Alzheimer's disease (AD). In vitro studies indicate that the 40-to 42-residue Aβ peptide in …

Amyloid fibrils and amorphous aggregates are two types of aberrant aggregates associated
with protein misfolding diseases. Although they differ in morphology, the two forms are often …

Self-assembly of amyloid fibrils is the molecular mechanism best known for its connection
with debilitating human disorders such as Alzheimer's disease but is also associated with …

We investigated the mechanisms of amyloidlike aggregation and gel formation in hen egg-
white lysozyme (HEWL) in a mixed solvent comprising 90% v/v ethanol in water using …

The aggregation of proteins and peptides in the form of stable and highly ordered amyloid
fibrils is most commonly associated with pathological conditions such as Alzheimer's …

Hydrogels of amyloid fibrils are a versatile biomaterial for tissue engineering and other
biomedical applications. Their suitability for these applications has been partly ascribed to …