<p>Binary metal-organic framework embellished magnetic black phosphorus nanosheets (Fe<sub>3</sub>O<sub>4</sub>/BPNSs/Ce-Zr MOF) were successfully prepared. This synthesis strategy avoided the traditional reliance on chelating agents and simplified the synthesis process. The physicochemical properties of Fe<sub>3</sub>O<sub>4</sub>/BPNSs/Ce-Zr MOF were systematically characterized by various means, such as transmission electron microscopy and X-ray diffraction analysis. The prepared material exhibited a high surface area, good hydrophilicity, and rapid magnetic responsiveness. Fe<sub>3</sub>O<sub>4</sub>/BPNSs/Ce-Zr MOF showed good affinity, which allowed the efficient capture of phosphopeptides from complex samples containing 5000-fold interfering peptides. Furthermore, Fe<sub>3</sub>O<sub>4</sub>/BPNSs/Ce-Zr MOF was applied to enrich phosphopeptides from more complicated biosamples, such as A549 cell lysate, highlighting its potential in phosphoproteomics applications.</p> Graphical abstract <p></p>

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Exploitation of binary metal-organic framework embellished magnetic black phosphorus nanosheets for phosphoproteome analysis

  • Dandan Jiang,
  • Yangyang Li,
  • Lan Lan

摘要

Binary metal-organic framework embellished magnetic black phosphorus nanosheets (Fe3O4/BPNSs/Ce-Zr MOF) were successfully prepared. This synthesis strategy avoided the traditional reliance on chelating agents and simplified the synthesis process. The physicochemical properties of Fe3O4/BPNSs/Ce-Zr MOF were systematically characterized by various means, such as transmission electron microscopy and X-ray diffraction analysis. The prepared material exhibited a high surface area, good hydrophilicity, and rapid magnetic responsiveness. Fe3O4/BPNSs/Ce-Zr MOF showed good affinity, which allowed the efficient capture of phosphopeptides from complex samples containing 5000-fold interfering peptides. Furthermore, Fe3O4/BPNSs/Ce-Zr MOF was applied to enrich phosphopeptides from more complicated biosamples, such as A549 cell lysate, highlighting its potential in phosphoproteomics applications.

Graphical abstract