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.
Thus far, each one has proved capable of
forming fibrils when heated or immersed in a solution containing acid or a form of alcohol.
This was the first time this technology has been used on amyloid fibrils of the infectious prion, which are a special form of clumped - together proteins that
form fibrils.
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.
Using microscopy, Tanzi, Moir, and their colleagues observed that amyloid - β
formed fibrils and trapped C. albicans cells in the guts of infected worms.
Not exact matches
Co-lead researcher, Australian National University Professor John Carver, said that two unrelated proteins aggregate in UHT milk over a period of months to
form clusters called amyloid
fibrils, which cause the milk to transform from a liquid into a gel.
«When a myocilin propellor misfolds, it unravels and
forms amyloid
fibrils (stringy abnormal proteins) that kill cells that maintain the trabecular network,» Lieberman said.
Chris Dobson, a chemist and structural biologist at the University of Cambridge, U.K., suspected that a much broader range of proteins could
form amyloid
fibrils in test tubes.
Materials scientist Robert Haddon has demonstrated that the bone -
forming mineral hydroxyapatite will grow around a nanotube scaffold, replacing the collagen
fibrils that grow naturally.
About 20 proteins share the ability to clump together to
form distinctive «amyloid
fibrils» that contribute to Alzheimer's, Creutzfeldt - Jakob disease, and a variety of lesser - known disorders.
An earlier study indicated that the intermediate step was likely a floppy loop area
formed by proteins, which didn't seem compatible with the tough, damaging
fibril as an end result.
The final β - sheets bind together and stack up to
form the damaging
fibrils.
Such
fibrils form plaques, or areas of tissue damage, that researchers can observe with microscopes.
And since the
fibrils they
form when misfolded are strong, scientists believe that hope primarily lies not in dismantling them, but in heading off the folding errors.
More than 40 illnesses known as amyloid diseases — Alzheimer's, Parkinson's and rheumatoid arthritis are a few — are linked to the buildup of proteins after they have transformed from their normally folded, biologically active
forms to abnormally folded, grouped deposits called
fibrils or plaques.
Chief among the
fibril forming collagens, type - I collagen gives many soft tissues strength and structure.
To do so, they engineered a collection of 20 DNA double helices to
form a nanotube big enough (15 to 20 nanometers — just over one - billionth of a meter — in diameter) to house the
fibrils.
«
Fibrils are remarkably strong and, as such, are a good barometer for this method's ability to
form two - dimensional structures,» observes Seeman.
In the past, he said, much research on Alzheimer's and similar disease focused on
fibrils, large bundles of misfolded proteins that
form in the brain.
Elongated fibres (
fibrils) of the beta - amyloid protein
form the typical senile plaques present in the brains of patients with Alzheimer's disease.
However,
fibrils are elongated structures that adhere to each other and neither
form crystals, nor can be dissolved in water.
This peptide, 39 to 42 amino acids long, is toxic to nerve cells and is able to
form elongated
fibrils.
Further immunological examinations show that the investigated
form of the
fibrils is especially relevant to the illness.
«NMR enabled us to obtain additional information such as which amino acid residues
form salt bridges thus enhancing the stability of the
fibrils,» explains Prof. Henrike Heise from Heinrich Heine University Düsseldorf and Jülich's Biomolecular NMR Center.
Tau and Mcc were induced to
form amyloid aggregates by incubation in buffer, and amyloid
fibril formation was characterized by ThT and transmission electron microscopy (Fig.
And that sequence can
form long chains called oligomers as well as fibers called
fibrils.
Amyloid - β 42 (Aβ42) has a strong ability to oligomerize to
form diffusible oligomers as well as larger polymers called
fibrils that
form insoluble amyloid plaques, a major hallmark of AD.
Four of the mAbs, 2T5C9, 2G9C, T1F11, and TB2H7, demonstrated diagnostic potential in enzyme - linked immunosorbent assays (ELISA) by their low to sub-nanomolar cross-reactivity with recombinant wild - type (WT) and mutant TTR aggregates and lack of binding to native TTR or amyloid
fibrils formed by other peptides or proteins.
To address this, we have generated 22 monoclonal antibodies (mAbs) against aggregates
formed by a blood transport protein, transthyretin (TTR), which primarily
forms amyloid
fibrils in a patient's heart and / or peripheral nerves.
This toxicity is mediated by the fibrillar
form of the amylin peptide and requires direct contact of the
fibrils with the cell surface.
The mutant
form, though,
forms amyloid
fibrils, as many proteins will do under the right (wrong?)
In recent years, scientists made the surprising discovery that seminal fluid harbors fragments of proteins that clump together,
forming structures called amyloid
fibrils.
Clumps that
form from these disease proteins are composed of sticky
fibrils that damage nerve cells.
They found that abnormal clumps of α - Syn
formed by small
fibrils act as «seeds» that induce normal α - Syn molecules to misfold and
form aggregates.
The basic building blocks of bone are collagen
fibrils that
form a latticework for deposition of calcium phosphate and other minerals.