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Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation

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  • Shu-Hsiang Huang
  • Shyue-Chu Ke
  • Ta-Hsin Lin
  • Hsin-Bin Huang
  • Yi-Cheng Chen

Abstract

Many properties of Aβ such as toxicity, aggregation and ROS formation are modulated by Cu2+. Previously, the coordination configuration and interaction of Cu2+ with the Aβ N-terminus has been extensively studied. However, the effect of Aβ C-terminal residues on related properties is still unclear. In the present study, several C-terminus-truncated Aβ peptides, including Aβ1-40, Aβ1-35, Aβ1-29, Aβ1-24 and Aβ1-16, were synthesized to characterize the effect of Aβ C-terminal residues on Cu2+ binding affinity, structure, aggregation ability and ROS formation. Results show that the Aβ C-terminal residues have effect on Cu2+ binding affinity, aggregation ability and inhibitory ability of ROS formation. Compared to the key residues responsible for Aβ 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 Aβ in the presence of Cu2+.

Suggested Citation

  • Shu-Hsiang Huang & Shyue-Chu Ke & Ta-Hsin Lin & Hsin-Bin Huang & Yi-Cheng Chen, 2014. "Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation," PLOS ONE, Public Library of Science, vol. 9(3), pages 1-10, March.
    • Handle: RePEc:plo:pone00:0090385
    DOI: 10.1371/journal.pone.0090385
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