Welcome to Journal of University of Chinese Academy of Sciences,Today is

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

  • YAO Fu-Jun ,
  • CUI Hong ,
  • LI Xiang-Jun
Expand
  • College of Chemistry and Chemical Engineering, Graduate University, Chinese Academy of Sciences, Beijing 100049, China

Received date: 2012-04-19

  Revised date: 2012-05-02

  Online published: 2012-05-02

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.

Cite this article

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]. Journal of University of Chinese Academy of Sciences, 2013 , 30(3) : 317 -321 . DOI: 10.7523/j.issn.1002-1175.2013.03.006

References

[1] Faller P, Hureau C. Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide[J]. Dalton Trans, 2009, 7: 1080-1094.

[2] Mattson M P. Pathways towards and away from Alzheimers disease[J]. Nature, 2004, 430(7000): 631-639.

[3] Selkoe D J. Cell biology of protein misfolding: the examples of Alzheimers and Parkinsons diseases[J]. Nat Cell Biol, 2004, 6(11): 1054-1061.

[4] Haass C, Selkoe D J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimers amyloid β-peptide[J]. Nat Rev Mol Cell Biol, 2007, 8(2): 101-112.

[5] Tanzi R E, Bertram L. Twenty years of the Alzheimers disease amyloid hypothesis: a genetic perspective[J]. Cell, 2005, 120(4): 545-555.

[6] Roychaudhuri R, Yang M, Hoshi M M, et al. Amyloid β-protein assembly and Alzheimer disease[J]. J Biol Chem, 2009, 284(8): 4749-4753.

[7] Chen T, Wang X, He Y, et al. Effects of cyclen and cyclam on zinc(II)- and copper(II)-induced amyloid β-peptide aggregation and neurotoxicity[J]. Inorg Chem, 2009, 48(13): 5801-5809.

[8] Huang X, Atwood C S, Moir R D, et al. Zinc-induced Alzheimers Aβ1-40 aggregation is mediated by conformational factors[J]. J Biol Chem, 1997, 272(42): 26464-26470.

[9] Sarell C J, Syme C D, Rigby S E, et al. Copper(II) binding to amyloid-β fibrils of Alzheimers disease reveals a picomolar affinity: stoichiometry and coordination geometry are independent of Aβ oligomeric form[J]. Biochemistry, 2009, 48(20): 4388-4402.

[10] Lovell M A, Robertson J D, Teesdale W J, et al. Copper, iron and zinc in Alzheimers disease senile plaques[J]. J Neurol Sci, 1998, 158(1): 47-52.

[11] Sabella S, Quaglia M, Lanni C, et al. Capillary electrophoresis studies on the aggregation process of β-amyloid 1-42 and 1-40 peptides[J]. Electrophoresis, 2004, 25(18-19): 3186-3194.

[12] Verpillot R, Esselmann H, Mohamadi M R, et al. Analysis of amyloid-β peptides in cerebrospinal fluid samples by capillary electrophoresis coupled with LIF detection[J]. Anal Chem, 2011, 83(5): 1696-1703.

[13] Colombo R, Carotti A, Catto M, et al. CE can identify small molecules that selectively target soluble oligomers of amyloid β protein and display antifibrillogenic activity[J]. Electrophoresis, 2009, 30(8): 1418-1429.

[14] Brambilla D, Verpillot R, Taverna M, et al. New method based on capillary electrophoresis with laser-induced fluorescence detetion(CE-LIF) to monitor interaction between nanoparticles and the amyloid-β peptide[J]. Anal Chem, 2010, 82(24): 10083-10089.

[15] Kozin S A, Zirah S, Rebuffat S, et al. Zinc binding to Alzheimers Aβ(1-16) peptide results in stable soluble complex[J]. Biochem Biophys Res Commun, 2001, 285(4): 959-964.

[16] Barnham K J, Cappai R, Beyreuther K, et al. Delineating common molecular mechanisms in Alzheimers and prion diseases[J]. Trends Biochem Sci, 2006, 31(8): 465-472.

[17] Murakami K, Irie K, Ohigashi H, et al. Formation and stabilization model of the 42-mer Aβ radical: implications for the long-lasting oxidative stress in Alzheimers disease[J]. J Am Chem Soc, 2005, 127(43): 15168-15174.

[18] Simth D G, Cappai R, Barnham K J. The redox chemistry of the Alzheimers disease amyloid β-peptide[J]. Biochim Biophys Acta, 2007, 1768(8): 1976-1990.

Outlines

/