Citation: ZHOU Si,  PENG Yu,  CHEN Yan-Ping,  JIA Qiong. Enrichment of Phosphopeptides with Quaternarized Magnetic Chitosan Composite[J]. Chinese Journal of Analytical Chemistry, ;2023, 51(6): 1051-1058. doi: 10.19756/j.issn.0253-3820.231052 shu

Enrichment of Phosphopeptides with Quaternarized Magnetic Chitosan Composite

  • Corresponding author: JIA Qiong, jiaqiong@jlu.edu.cn
  • Received Date: 15 February 2023
    Revised Date: 31 March 2023

    Fund Project: Supported by the State Key Laboratory of Inorganic Synthesis & Preparative Chemistry, Jilin University (No. 2022-21).

  • Protein phosphorylation is one of the most important and common post-translational modifications, and the determination of protein phosphorylation is essential for comprehensive understanding of phosphorylation pathways in biological processes. Mass spectrometric technique has become an important method to analyze protein phosphorylation. However, the low abundance, low ionization efficiency of phosphopeptides and their coexistence with non-phosphopeptides seriously affect the direct analysis of phosphopeptides by mass spectrometry. To solve this issue, selective enrichment of phosphopeptides is usually required before the analysis step. Functional magnetic materials have good magnetic responsiveness and can be quickly separated from solution with the help of external magnets. In the present work, a new method based on quaternarized magnetic chitosan composite as the adsorbent was developed for enrichment of phosphopeptides combined with matrixassisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). The magnetic material had the advantages such as rapid magnetic response, good biocompatibility, positive electricity, cheap availability, and good enrichment selectivity for phosphopeptides. The detection limit of β-casein was 0.4 fmol after enrichment. This method was successfully applied to detection of phosphopeptides in actual skim milk samples, indicating that the synthesized magnetic material had high application potential in detection of phosphopeptides in complex samples.
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