Author： El-Agnaf O.M.A.
Publisher： Ios Press
ISSN： 0712-4813
Source： Spectroscopy, Vol.15, Iss.3-4, 2001-01, pp. : 141-150
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Abstract
Experiments on fragments of NAC have enabled the region of NAC responsible for its aggregation and toxicity to be identified.
-Synuclein has been identified as a component of intracellular fibrillar protein deposits in several neurodegenerative diseases, and two mutant forms have been associated with early onset Parkinson's disease. A fragment of -synuclein has also been identified as the non-A
component of Alzheimer's disease amyloid (NAC). Ageing solutions of -synuclein and NAC leads to formation of -sheet, detectable by circular dichroism spectroscopy, and aggregation to form amyloid-like fibrils, detectable by electron microscopy. Differences in the rates of aggregation of the fibrils formed by -synuclein and the two mutant proteins are presented. The toxicity of -synuclein and related peptides towards neurons is also discussing in relation to the aetiology of neurodegenerative diseases.
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