Not exact matches
While these compounds did not reduce the amount of protein aggregates, they were found to reduce the protein's toxicity and to increase the stability of amyloid
fibrils — a finding that lends further evidence to the theory that smaller assemblies of amyloid -
beta known as oligomers, and not the
fibrils themselves, are the toxic agents responsible for Alzheimer's symptoms.
«They all exhibit variations of their secondary structure — describes Iban Amenabar, who performed the nanospectroscopy experiments -; viruses and ferritin are mainly made of alpha - helical structures, while insulin
fibrils are mainly made of
beta - sheet structures.»
In close collaboration with his TUM colleagues Johannes Buchner, professor of biotechnology and Sevil Weinkauf, professor of electron microscopy, Reif determined that the small heat shock protein uses a specific non-polar
beta - sheet structure pile in its center for interactions with the
beta - amyloid, allowing it to access the aggregation process in two locations at once: For one it attaches to individual dissolved
beta - amyloids, preventing them from forming
fibrils.
If the newly discovered
beta - sheet structure idea could be integrated as building blocks into such artificially designed proteins, it would improve their ability to attach to the disease - causing
fibrils — a first step in the development of new agents against Alzheimer's and other neurodegenerative diseases.
Elongated fibres (
fibrils) of the
beta - amyloid protein form the typical senile plaques present in the brains of patients with Alzheimer's disease.
The
fibrils of the body's own amyloid
beta (Aβ) protein are the main constituent of Alzheimer's disease related and characteristic pathological protein deposits in the brain.
A European research team and a team from the United States (Massachussetts Institute of Technology in cooperation with Lund University) have simultaneously succeeded in elucidating the structure of the most disease - relevant
beta - amyloid peptide 1 - 42
fibrils at atomic resolution.
The amyloid -
beta bound itself to C. albicans and grew
fibrils that entombed the fungal invader — and as part of that process, created plaques of amyloid -
beta.
In view of the fact that the
beta - amyloid protein that forms
fibrils in Alzheimer's disease is toxic to neurons, we have investigated whether amylin
fibrils could be toxic to pancreatic islet cells.
The reactivity of this monoclonal antibody was not dependent on the V (L) or C (L) isotype of the
fibril, but rather seemed to be directed toward a
beta - pleated sheet conformational epitope expressed by AL and other amyloid proteins.
These reagents, prepared against human light chain - related
fibrils, recognize an epitope common to the
beta - pleated structure of AL and other types of amyloid proteins and can effect rapid amyloidolysis when administered to mice injected with human AL amyloid extracts.
Curcumin has potent anti-amyloidogenic effects for Alzheimer's
beta - amyloid
fibrils in vitro.