Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …

Amyloid refers to insoluble protein aggregates that are responsible for amyloid diseases but
are also implicated in important physiological functions (functional amyloids). The …

Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common
properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and …

Background Protein aggregation correlates with the development of several debilitating
human disorders of growing incidence, such as Alzheimer's and Parkinson's diseases. On …

We describe solid-state nuclear magnetic resonance (NMR) measurements on fibrils formed
by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ1-40) that …

Recent reports give strong support to the idea that amyloid fibril formation and the
subsequent development of protein deposition diseases originate from conformational …

The presence of β‐sheets in the core of amyloid fibrils raised questions as to whether or not
β‐sheet‐containing proteins, such as transthyretin, are predisposed to form such fibrils …

Motivation: Amyloidogenic regions in polypeptide chains are very important because such
regions are responsible for amyloid formation and aggregation. It is useful to be able to …

We report the detailed mechanical characterization of individual amyloid fibrils by atomic
force microscopy and spectroscopy. These self-assembling materials, formed here from the …

Diffusible subfibrillar aggregates of amyloid proteins are potent neurotoxins and primary
suspects in amyloid diseases including Alzheimer's disease. Despite widespread interest …