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Abstract: Protein phosphorylation is one of the most important post-translational modifications involved in the regulation of various cellular processes. Selective capture of phosphopeptides from complex biological samples is essential prior to mass spectrometry (MS) analysis of protein phosphorylation. Herein, pyrophosphate-imprinted magnetic affinity microspheres composed of a magnetic Fe3O4 core and pyrophosphate-imprinted mesoporous silica shell have been facilely synthesized through the combination of a surfactant-templated sol-gel process and a dual-template docking oriented molecular imprinting process. They have a relatively large specific surface area (142.1 m2 g-1) and superparamagnetism with a saturation magnetization (Ms) value (66.54 emu g-1). In virtue of their selective affinity with molecular recognition, porous structure and strong magnetism, they can realize the rapid and effective purification of phosphopeptides from real biosamples for MS analysis. These results reveal that this work will be beneficial for future applications in the fast magnetic isolation and specific identification of phosphorylated biomolecules
Template and target information: pyrophosphate, phosphopeptides
Author keywords: enrichment, imprinting, magnetic properties, mesoporous materials, Phosphopeptide