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Updated: Jun 28, 2026
Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery
Published on: April 17, 2012
Design of Ce3+ ions functionalized magnetic black phosphorus nanosheets for highly efficient enrichment of
Dandan Jiang1, Yangyang Li1, Siyu Wu1
1Inner Mongolia Engineering Research Centre of Lithium-Sulfur Battery Energy Storage, Inner Mongolia Key Laboratory of Carbon Nanomaterials, Nano Innovation Institute (NII), College of Chemistry and Materials Science, Inner Mongolia Minzu University, Tongliao, 028000, PR China.
Background:
The abnormal variation of phosphorylation can lead to many human diseases, such as Alzheimer's disease and cancer. Because of its high throughput and rapidity, mass spectrometry (MS)-based method has been widely used to characterize phosphopeptides/phosphoproteins in complex biological samples. However, the direct MS analysis for phosphopeptides is still a challenging task due to the complexity of biological samples and the signal suppression of abundant non-phosphopeptides. Therefore, an efficient enrichment platform for low-abundance phosphopeptide capture and detection is in great demand.
Results:
In this study, Ce3+ ions functionalized magnetic black phosphorus nanosheets were successfully synthesized and characterized. The prepared magnetic material had high surface area (185.80 m2 g-1), good hydrophilicity (12.15°), and magnetic property (33.38 emu g-1). The magnetic material provided abundant affinity sites for phosphopeptide enrichment through immobilized metal ion affinity chromatography (IMAC). By combining MS analysis, the method exhibited satisfactory performance, including high sensitivity (0.1 fmol), good selectivity (α-casein: β-casein: BSA = 1: 1: 5000), and high recovery (87.2 %). The method was applied to enrich and detect phosphopeptides in skimmed milk, human saliva, serum, and A549 cell lysate, proving its feasibility for phosphopeptide analysis. Additionally, the method provided the sequence motifs of the captured phosphopeptides and the biological functions of the phosphoproteins in A549 cell lysate.
Significance:
This work presented a facile analysis platform for phosphopeptides, including sample preparation, enrichment process, and MS detection. The analysis strategy was successfully adopted for capturing and analyzing phosphopeptides from stranded proteins and complex bio-samples. This work presents a novel approach for the design and construction of black phosphorus-based adsorbents in phosphoproteomics research.
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