摘要: A plethora of clinical syndromes are characterized by the deposition amorphous, Congo red staining material known as “amyloid.” These protein folding diseases include Alzheimer’s, Parkinson’s, type II diabetes mellitus, rheumatoid arthritis, and “mad cow” disease. Amyloid-forming peptides readily adapt beta-sheet structure can spontaneously aggregate into extended fibrils despite having no primary sequence homology. All amyloid appear to interact strongly with lipid membranes, assemble oligomers, form ion-permeable channels. channels large, heterogeneous, nonselective, irreversible. They inhibited blocked Zn+2. The leakage pathway induced these could be responsible for cellular pathology amyloidoses, including membrane depolarization, mitochondrial dysfunction, inhibition long-term potential (LTP), cytotoxicity. We suggest that channel formation underlies
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