Multiple ligand interaction of α-synuclein produced various forms of protein aggregates in the presence of Aβ25-35, copper, and eosin

Abstract

Various protein aggregates of α-synuclein developed by way of the common protein self-oligomerization in the presence of Aβ25-35, 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.