4.6 Article

Phytic acid functionalized magnetic bimetallic metal-organic frameworks for phosphopeptide enrichment

Journal

JOURNAL OF MATERIALS CHEMISTRY B
Volume 9, Issue 7, Pages 1811-1820

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/d0tb02517h

Keywords

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Funding

  1. National Natural Science Foundation of China [31771037, 51673124]
  2. National Key Research and Development Program of China [2016YFC1102701]
  3. Sichuan University Interdisciplinary Cross-disciplinary Research Program [2020KXK0401]

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A novel magnetic bimetallic metal-organic framework nanocomposite was successfully fabricated for highly sensitive and selective enrichment of phosphopeptides from complex biological samples. The nanomaterial exhibited good reusability and identified multiple phosphopeptides in biological samples, showing great potential for further analysis of low abundance phosphopeptides.
Highly specific enrichment of phosphopeptides from complex biological samples was a precondition for further studying its physiological and pathological processes due to the important and trace amounts of phosphopeptides. In this work, phytic acid (PA) functionalized magnetic cerium and zirconium bimetallic metal-organic framework nanocomposites (denoted as Fe3O4@SiO2@Ce-Zr-MOF@PA) were fabricated by a facile yet efficient method. The as-prepared nanomaterial exhibited high sensitivity (0.1 fmol mu L-1), high selectivity toward phosphopeptides from beta-casein tryptic digests/BSA (1 : 800), and good reusability of five cycles for enriching phosphopeptides. This affinity probe was applied to biological samples, and 19, 4 and 15 phosphopeptides were identified from non-fat milk, human serum and human saliva, respectively. The above marked advantages are attributed to the strong affinity of the abundant Ce-O and Zr-O nanoclusters on the surface of the MOF shell with the improved hydrophilicity from a great number of phosphate groups. Therefore, the novel Fe3O4@SiO2@Ce-Zr-MOF@PA nanospheres could not only enrich phosphopeptides effectively, but also reduce the adsorption of phosphopeptides, manifesting great potential in the identification and further analysis of low abundance phosphopeptides in complex biological samples.

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