The aggregation of proteins is central to many aspects of daily life, including food
processing, blood coagulation, eye cataract formation disease and prion-related …

Aggregation of amyloidogenic proteins into insoluble amyloid fibrils is implicated in various
neurodegenerative diseases. This process involves protein assembly into oligomeric …

Amyloid fibrils are proteinaceous nano-scale linear aggregates. They are of key interest not
only because of their association with numerous disorders, such as type II diabetes mellitus …

Protein fibrils are a crucial subject of study in various research fields and disciplines.
Amyloid fibrils are highly ordered fibrillar structures assembled from either peptides or …

Using atomic force microscopy height maps, we resolve and quantify torsional fluctuations in
one-dimensional amyloid fibril aggregates self-assembled from three different …

Atomic force microscopy has been employed to investigate the structural organization of
amyloid fibrils produced in vitro from three very different polypeptide sequences. The …

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

The development of atomic force microscopy (AFM) has opened up a wide range of novel
opportunities in nanoscience and new modalities of observation in complex biological …

Amyloid β-protein (Aβ) oligomers are emerging as potent neurotoxic species in Alzheimer's
disease pathogenesis. Detailed characterization of oligomer structure and dynamics is …

Late-onset diabetes is typically associated with amyloid deposits of fibrillar amylin in the
pancreatic islets. Aqueous synthetic human amylin spontaneously forms polymorphic fibrils …