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amyloid beta
(Aβ, Abeta)
Peptides of 36-43 amino acids, a by-product generated as the result of proteolytic processing of the amyloid precursor protein cleaved by beta and gamma secretases.
Amyloid-beta precursor protein is an integral membrane protein expressed in many tissues and concentrated in the synapses of neurons. It functions as a cell surface receptor and plays roles as a regulator of synapse formation, neural plasticity, antimicrobial activity, and iron export.
Proteins are large, exquisitely folded molecules that play essential and diverse roles in the living organisms and must achieve and retain a specific 3-dimensional conformation in order to function properly.
If protein folding is disrupted, proteins can display sticky surfaces and aggregate through several stages eventually assembling into fibers. Such nonfunctional protein aggregates can be toxic. Protein misfolding diseases are found in multiple organs, and can be defined by the presence of specific misfolded protein deposits.
Amyloid beta molecules can aggregate to form misfolded oligomers and develop into amyloid fibrils.
The chain reaction to form such larger structures is similar to other protein misfolding diseases such as a prion infection.
Alzheimer's disease and Parkinson's disease are caused by the formation of amyloid plaques and neurofibrillary tangles.
(How to reduce amyloid beta)
• Insulin-degrading enzyme can degrade amyloid beta.
• Silica nanoparticles tightly adsorb amyloid beta aggregates without altering their native aggregation-driving domains and remove them out of the cell membrane.
• Gamma wave stimulation in a combination of light and sound does not only reduce levels of beta amyloid and tau proteins associated with Alzheimer's disease but also boosts the activity of microglia in clearing harmful debris.
Cf. systemic amyloidosis
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