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Mass spectrometric analysis of mono- and multi-phosphopeptides by selective binding with NiZnFe2O4 magnetic nanoparticles

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  • Hongying Zhong

    (Key Laboratory of Pesticides and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University)

  • Xiao Xiao

    (Key Laboratory of Pesticides and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University)

  • Shi Zheng

    (Key Laboratory of Pesticides and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University)

  • Wenyang Zhang

    (Key Laboratory of Pesticides and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University)

  • Mengjie Ding

    (Key Laboratory of Pesticides and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University)

  • Haiying Jiang

    (Key Laboratory of Pesticides and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University)

  • Lulu Huang

    (Key Laboratory of Pesticides and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University)

  • Jie Kang

    (Key Laboratory of Pesticides and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University)

Abstract

Selective isolation of mono- and multi-phosphorylated peptides is important for understanding how a graded protein kinase or phosphatase signal can precisely modulate the on and off states of signal transduction pathways. Here we report that metal ions at exposed octahedral sites of nano-ferrites, including Fe3O4, NiFe2O4, ZnFe2O4 and NiZnFe2O4, have distinctly selective coordination abilities with mono- and multi- phosphopeptides. Due to their intrinsic magnetic properties and high surface area to volume ratios, these nanoparticles enable the rapid isolation of mono- and multi-phosphopeptides by an external magnetic field. Model phosphoprotein α-casein and two synthesized mono- and di-phosphopeptides have been chosen for proof-of-principle demonstrations, and these nanoparticles have also been applied to phosphoproteome profiling of zebrafish eggs. It is shown that NiZnFe2O4 is highly selective for multi-phosphopeptides. In contrast, Fe3O4, NiFe2O4 and ZnFe2O4 can bind with both mono- and multi-phosphopeptides with relatively stronger affinity towards mono-phosphopeptides.

Suggested Citation

  • Hongying Zhong & Xiao Xiao & Shi Zheng & Wenyang Zhang & Mengjie Ding & Haiying Jiang & Lulu Huang & Jie Kang, 2013. "Mass spectrometric analysis of mono- and multi-phosphopeptides by selective binding with NiZnFe2O4 magnetic nanoparticles," Nature Communications, Nature, vol. 4(1), pages 1-7, June.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2662
    DOI: 10.1038/ncomms2662
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