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中国科学院大学学报 ›› 2013, Vol. 30 ›› Issue (3): 317-321.DOI: 10.7523/j.issn.1002-1175.2013.03.006

• 化学与生命科学 • 上一篇    下一篇

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

姚付军, 崔宏, 李向军   

  1. 中国科学院研究生院化学与化学工程学院, 北京 100049
  • 收稿日期:2012-04-19 修回日期:2012-05-02 发布日期:2013-05-15
  • 通讯作者: 李向军, lixiangj@ucas.ac.cn
  • 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

YAO Fu-Jun, CUI Hong, LI Xiang-Jun   

  1. College of Chemistry and Chemical Engineering, Graduate University, Chinese Academy of Sciences, Beijing 100049, China
  • Received:2012-04-19 Revised:2012-05-02 Published:2013-05-15

摘要:

β-淀粉样蛋白(Aβ)的聚集及纤维生成与阿尔茨海默病(AD)存在密切的关系,大量证据表明,老年斑中含有高浓度的过渡金属离子如Zn2+、Cu2+和Fe3+. 本文采用高效毛细管电泳法(HPCE-UV)研究金属离子与Aβ16以及Aβ28的相互作用. 研究表明,Zn2+、Cu2+和Fe3+都可以与Aβ发生相互作用,但Cu2+可以诱导Aβ16的聚集生成低聚体而Zn2+不能. Zn2+和Fe3+都可以诱导Aβ28生成低聚体,但聚集的速率不同.

关键词: 毛细管电泳, &beta, 淀粉样蛋白, 金属离子, 相互作用

Abstract:

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.

Key words: high-performance capillary electrophoresis, amyloid-&beta, peptide, metal ions, interaction

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