title: Effect of C-terminal residues of Aβ on copper binding affinity, structural conversion and aggregation.
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+.
authors.affiliation: Department of Medicine, MacKay Medical College, New Taipei City, Taiwan.
authors.forename: Shu-Hsiang
authors.initials: SH
authors.lastname: Huang
authors.affiliation: Department of Physics, National Dong Hwa University, Hualien, Taiwan.
authors.forename: Shyue-Chu
authors.initials: SC
authors.lastname: Ke
authors.affiliation: Department of Medical Research & Education, Taipei Veterans General Hospital, Taipei city, Taiwan; Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan.
authors.forename: Ta-Hsin
authors.initials: TH
authors.lastname: Lin
authors.affiliation: Institute of Molecular Biology, National Chung-Cheng University, Chiayi, Taiwan.
authors.forename: Hsin-Bin
authors.initials: HB
authors.lastname: Huang
authors.affiliation: Department of Medicine, MacKay Medical College, New Taipei City, Taiwan.
authors.forename: Yi-Cheng
authors.initials: YC
authors.lastname: Chen
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D002942:Circular Dichroism; D003300:Copper / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D046529:Microscopy, Electron, Transmission; D017433:Protein Structure, Secondary; D017382:Reactive Oxygen Species / Q000378:metabolism; D013050:Spectrometry, Fluorescence
chemical_list: D016229:Amyloid beta-Peptides; D017382:Reactive Oxygen Species; D003300:Copper