Citation: ZHAO Yan-Yan, ZHANG Li-Hua, ZHANG Li-Yuan. Preparation of Novel Zirconium Ion immobilized Affinity Magnetic Nanoparticles and Application in Efficient Capture of Phosphopeptides[J]. Chinese Journal of Analytical Chemistry, ;2020, 48(2): 233-239. doi: 10.19756/j.issn.0253-3820.191681 shu

Preparation of Novel Zirconium Ion immobilized Affinity Magnetic Nanoparticles and Application in Efficient Capture of Phosphopeptides

1.
College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China;
2.
CAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China;
3.
College of Pharmacy, Dalian Medical University, Dalian 116044, China

Received Date: 18 November 2019
Revised Date: 19 December 2019

Fund Project: This work was supported by the National Natural Science Foundation of China (Nos. 21974017, 21505015), the Project of CAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, the Program in Liaoning Province Education Department (No. LZ2019063), the Natural Science Foundation of Liaoning Province, China (No. 20170540286), and the Dalian High-level Talents Innovation Support Program (No. 20170540286).

Protein phosphorylation is one of the most common and important post-translational modifications, which plays key regulatory roles in biological processes, such as cell signaling and apoptosis. However, due to the low abundance and negative charge of phosphorylated proteins, in the conventional positive ion mode of bio-mass spectrometry, phosphoproteins are susceptible to be suppressed by high-abundance non-phosphorylated proteins, making them difficult to be directly analyzed. Therefore, the enrichment of phosphorylated proteins/peptides prior to mass spectrometry is important in biological research. For the first time, in this study, a novel zirconium ion-immobilized affinity magnetic nanoparticle (Zr⁴⁺-ATP-MNP) was prepared using adenosine triphosphate (ATP) as the ligand. The ATP ligand in Zr⁴⁺-ATP-MNP contains three phosphate groups, which can simultaneously provide multiple zirconium ion chelating sites, thus form stable network compounds with zirconium ions and provide high activity towards phosphorylated peptide. In addition, the hydrophilic pentose (ribose) and purine (adenine) parts in the ATP structure can significantly increase the hydrophilicity of the material and reduce the non-specific adsorption from non-phosphorylated peptides. The results of scanning electron microscopy and elemental analysis indicated that Zr⁴⁺-ATP-MNP was successfully prepared. Using β-casein digest as the sample, 9 phosphopeptides were identified. From digest mixture of β-casein and BSA with molar ratio as low as 1:100, five phosphopeptides were effectively identified with significantly improved signal and the non-phosphorylated peptides were effectively removed. The above results demonstrated the high specificity of Zr⁴⁺-ATP-MNP for both monophosphorylated peptides and multiphosphorylated peptides. The Zr⁴⁺-ATP-MNP was further applied to capture phosphopeptides in milk digest. All these results indicated the promising potential of Zr⁴⁺-ATP-MNP to capture mono- and multi-phosphopeptides in complex biological samples.
- Immobilized affinity,
- Phosphopeptide,
- Enrichment,
- Magnetic
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