ABSTRACT
Many properties of Aß such as toxicity, aggregation and ROS formation are modulated by Cu2+. Previously, the coordination configuration and interaction of Cu2+ with the Aß N-terminus has been extensively studied. However, the effect of Aß C-terminal residues on related properties is still unclear. In the present study, several C-terminus-truncated Aß peptides, including Aß1-40, Aß1-35, Aß1-29, Aß1-24 and Aß1-16, were synthesized to characterize the effect of Aß C-terminal residues on Cu2+ binding affinity, structure, aggregation ability and ROS formation. Results show that the Aß C-terminal residues have effect on Cu2+ binding affinity, aggregation ability and inhibitory ability of ROS formation. Compared to the key residues responsible for Aß aggregation and structure in the absence of Cu2+, it is more likely that residues 36-40, rather than residues 17-21 and 30-35, play a key role on the related properties of Aß in the presence of Cu2+.
