We report here structural differences between Aβ (1-40) protofibrils and mature amyloid
fibrils associated with Alzheimer's disease as determined using hydrogen-deuterium …

Although the gross morphology of amyloid fibrils is fairly well understood, very little is known
about how the constituent polypeptides fold within the amyloid folding motif. In the …

We describe here experiments designed to characterize the secondary structure of amyloid
fibrils of the Alzheimer's amyloid plaque peptide Aβ, using hydrogen-deuterium exchange …

We describe electron microscopy (EM), scanning transmission electron microscopy (STEM),
and solid-state nuclear magnetic resonance (NMR) measurements on amyloid fibrils formed …

Although the amyloid fibrils formed from the Alzheimer's disease amyloid peptide Aβ are rich
in cross-β sheet, the peptide likely also exhibits turn and unstructured regions when it …

The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH2, called Aβ16-22
and representing residues 16− 22 of the full-length β-amyloid peptide associated with …

Protofibrils are transient structures observed during in vitro formation of mature amyloid
fibrils and have been implicated as the toxic species responsible for cell dysfunction and …

β-Amyloid peptide (Aβ) is the primary protein component of senile plaques in Alzheimer's
disease and is believed to be responsible for the neurodegeneration associated with the …

Some of the pathological hallmarks of the Alzheimer's disease brain are senile plaques
composed of insoluble amyloid-β protein (Aβ) fibrils. However, much of the recent emphasis …

Amyloid fibrils are fibrous polypeptide aggregates that can be formed in vitro and under
pathologic conditions, such as in type II diabetes, Alzheimer's and Creutzfeldt-Jakob …