文摘
Residue specific mapping of Cu2 + binding sites along with the strength and order of binding was studied in the wild type α-Syn and recently discovered familial mutants i.e. H50Q and G51D. The region 48-53 of H50Q does not bind to Cu2 +, unlike wild-type and G51D. Even though the binding of Cu2 + was less in H50Q, the rate of fibril formation was higher compared to the wild-type. The aggregation kinetics of the slower aggregating familial mutant G51D showed a significant decrease in the lag phase in the presence of Cu2 +. The H50Q fibrillar species were more toxic compared to the fibrillar species generated in the presence of Cu2 +, unlike wild-type.