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Amyloid is formed through the polymerization of hundreds to thousands of monomeric peptides or proteins into long fibers. Amyloid formation involves a lag phase (also called nucleation phase), an exponential phase (also called growth phase) and a plateau phase (also called saturation phase), as shown in the figure.
However, several aspects of amyloid biology are still under investigation. For example, recent evidence has suggested that amyloid plaque formation is linked to brain microvascular trauma. [49] [50] Other research implicates chronic inflammation of the brain and immune dysfunction of the nervous system. [51] [52]
Amyloid beta (Aβ, Abeta or beta-amyloid) denotes peptides of 36–43 amino acids that are the main component of the amyloid plaques found in the brains of people with Alzheimer's disease. [2] The peptides derive from the amyloid-beta precursor protein (APP), which is cleaved by beta secretase and gamma secretase to yield Aβ in a cholesterol ...
The Curli protein is a type of amyloid fiber produced by certain strains of enterobacteria. They are extracellular fibers located on bacteria such as E. coli and Salmonella spp. [2] These fibers serve to promote cell community behavior through biofilm formation in the extracellular matrix. Amyloids are associated with several human ...
When the vesicles are released, the amyloid grows as it collects even more IAPP outside the cell. The overall effect is an apoptosis cascade initiated by the influx of ions into the β-cells. General Scheme for Amyloid Formation. In summary, impaired N-terminal processing of proIAPP is an important factor initiating amyloid formation and β ...
Relates average packing density of residues to the formation of amyloid fibrils. sequence - Amyloidogenic regions Beta-strand contiguity [6] 2007 Web Server- AMYLPRED2: Phenomenological. Prediction of B-strand propensity score to locate in the amyloid fibril. sequence - beta-strand formation Hexapeptide Conformational Energy /Pre-amyl [7] 2007
There is evidence that eating amyloid fibers may lead to amyloidosis. This evidence is based on studies in cattle, chickens, mice, and cheetahs. [ 22 ] Thus, in a sense, SAA amyloidosis may be considered a contagious disease, although whether this occurs or is important in the development of naturally occurring amyloidosis remains unknown.
The alpha sheet has been proposed as a possible intermediate state in the conformational change in the formation of amyloid fibrils by peptides and proteins such as amyloid beta, poly-glutamine repeats, lysozyme, prion proteins, and transthyretin repeats, all of which are associated with protein misfolding disease.