收稿日期: 2012-04-19
修回日期: 2012-05-02
网络出版日期: 2012-05-02
基金资助
国家自然科学基金(21145006)、教育部归国学者科学研究基金和北京市自然科学基金(2113046)资助
Interactions of β-amyloid peptide with metal ions studied by means of high-performance capillary electrophoresis
Received date: 2012-04-19
Revised date: 2012-05-02
Online published: 2012-05-02
姚付军 , 崔宏 , 李向军 . 高效毛细管电泳法研究β-淀粉样蛋白与金属离子的相互作用[J]. 中国科学院大学学报, 2013 , 30(3) : 317 -321 . DOI: 10.7523/j.issn.1002-1175.2013.03.006
Aggregation of the peptide amyloid-β (Aβ) into fibrils is considered to be closely related to the cause of Alzheimer disease (AD). Transition metals, such as Cu(Ⅱ), Zn(Ⅱ), and Fe(Ⅲ), are found in Aβ plaques and shown to affect Aβ aggregation. We investigated the interactions between those metal ions and the peptide amyloids (Aβ16 and Aβ28) by high-performance capillary electrophoresis coupled with UV detection (HPCE-UV). The experiments show that (i) the Zn2+, Cu2+, and Fe3+ ions interact with Aβ; (ii) Cu2+ rather than Zn2+ accelerates the aggregation of Aβ16 and the formation of oligomers. In addition, Zn2+ and Fe3+ accelerate the aggregation of Aβ28 with different acceleration rates.
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