Journal
BRAIN RESEARCH
Volume 908, Issue 1, Pages 93-98Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0006-8993(01)02575-6
Keywords
alpha-synuclein; self-oligomerization; protein aggregation; cytotoxicity; Parkinson's disease
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Various protein aggregates of alpha -synuclein developed by way of the common protein self-oligomerization in the presence of A beta 25-35, copper, and eosin were examined. All the aggregates exhibited congo red birefringence although the actual amounts of the aggregates were varied as determined by thioflavin T binding fluorescence. When their morphologies were analyzed in relation to in vitro cytotoxicity, the smallest granular aggregates obtained with copper exhibited the highest cytotoxicity, while the fibrous structures by eosin did not affect the cell. (C) 2001 Elsevier Science B.V. All rights reserved.
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