Details

Autor(en) / Beteiligte

• Huang, Shu-Hsiang
• Ke, Shyue-Chu
• Lin, Ta-Hsin
• Huang, Hsin-Bin
• Chen, Yi-Cheng
• Permyakov, Eugene A.

Titel

Effect of C-terminal residues of Aβ on copper binding affinity, structural conversion and aggregation

Ist Teil von

• PloS one, 2014-03, Vol.9 (3), p.e90385-e90385

Ort / Verlag

United States: Public Library of Science

Erscheinungsjahr

2014

Quelle

Free E-Journal (出版社公開部分のみ）

Beschreibungen/Notizen

• 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+.