The researchers built a protein structure, called «alpha sheet,» that complements the toxic
structure of amyloid proteins that they discovered in computer simulations.
The molecular
structure of an amyloid protein can be only slightly different from a normal protein and can transform to a toxic state fairly easily, which is why amyloid diseases are so prevalent.
Not exact matches
An analysis
of the peptide's
structure in semen indicated that it hooked up with similar fragments to create
amyloid fibers (clusters
of protein fragments that have also been implicated in diseases such as Alzheimer's).
Armed with a precise knowledge
of the atomic
structure of the
amyloid - beta
protein, Jiang, Eisenberg and colleagues conducted a computational screening
of 18,000 compounds in search
of those most likely to bind tightly and effectively to the
protein.
An
amyloid fibril is a large
structure consisting
of misfolded
proteins.
We see manifold applications, such as studies
of conformational changes in
amyloid structures on the molecular level, the mapping
of nanoscale
protein modifications in biomedical tissue or the label - free mapping
of membrane
proteins.
«What's critical with this and what has never been done before is that a single peptide sequence will work against the toxic versions
of a number
of different
amyloid proteins and peptides, regardless
of their amino acid sequence or the normal 3 - D
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.
A plaque is an accumulation
of proteins that are primarily made up
of Amyloid beta (A-beta), a small
structure that splits off from the
Amyloid Precursor
Protein (APP).
Diamond and his colleagues have shown that a part
of nerve cells» inner
structure known as tau
protein can misfold into a configuration called an
amyloid.
The team found that the
Amyloid beta
proteins entered the cells
of the retina within 24 hours
of exposure and then began to break the cell's scaffold
structure.
This is a drawing representing
structure of properly functioning
protein (left) which is optically invisible to high power laser light, and toxic
amyloid (right) responsible for brain diseases that might potentially be cured using lasers in photo therapies.
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.
In recent years, scientists made the surprising discovery that seminal fluid harbors fragments
of proteins that clump together, forming
structures called
amyloid fibrils.
Amyloid fibers, those clumps
of plaque - like
proteins that clog up the brains
of Alzheimer's patients, have perplexed scientists with their robust
structures.
In the October 19, 2006, issue
of Nature (available online Oct. 11), the researchers describe the
structures of insulin - degrading enzyme (IDE) in complex with four
of the
proteins it digests: insulin,
amyloid - beta, amylin and glucagon.
Researchers from the University
of Chicago and Argonne National Laboratory have deciphered the three - dimensional
structure of insulin - degrading enzyme, a promising target for new drugs because it breaks down not only insulin but also the
amyloid - beta
protein, which has been linked to the cognitive decline
of Alzheimer's disease.