Interactions of β-amyloid peptide with metal ions studied by means of high-performance capillary electrophoresis

doi:10.7523/j.issn.1002-1175.2013.03.006

Abstract

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

CLC Number:

YAO Fu-Jun, CUI Hong, LI Xiang-Jun. Interactions of β-amyloid peptide with metal ions studied by means of high-performance capillary electrophoresis[J]. , 2013, 30(3): 317-321.

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