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<p>Protein phosphorylation is a common yet critical type of post-translational modification. The selective recognition and enrichment of phosphorylated peptides are essential for the structural identification of phosphorylated proteins and subsequent biomedical research. A method was developed using reversible addition-fragmentation chain transfer (RAFT) polymerization to graft a controllable imprinted polymer layer on the surface, enabling the recognition of phosphorylated angiotensin II (PAngII) via dummy template molecular imprinting technology with phenylphosphonic acid (PPA) as the template. After modifying silica particles with vinyl and disulfide groups, PPA and functional monomers were added to initiate polymerization reactions, forming a controllable polymer layer covalently attached to the silica particle surface. Effective imprinting sites were created through hydrogen bonding between the functional monomer allyl urea and PPA. Under RAFT regulation, the binding capacity for PPA was 0.372&#xa0;mg&#xa0;g<sup>–1</sup> with an imprinting factor (IF) of 2.12, while the binding capacity for PAngII was 0.719&#xa0;mg&#xa0;g<sup>–1</sup> with an IF of 1.86. These IF values were significantly higher than those obtained without RAFT regulation. Additionally, PAngII was recognized by the imprinted particles even in the presence of non-phosphorylated peptides. The recognized performance of PAngII remained at 93% after five cycles of adsorption&#xa0;and desorption. It was demonstrated that surface-grafted, controllable imprinted particles using a dummy template and RAFT strategy show great promise for phosphopeptide recognition, exhibiting good selectivity and reusability.</p>

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Surface-grafted molecularly imprinted particles for phosphorylated angiotensin II recognition with dummy template strategy and reversible addition-fragmentation chain transfer polymerization

  • 期刊论文

  • 发表日期：

    2026年7月9日

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  • Zhen Fan,
  • Yongjian Wang,
  • Kejing Lv,
  • Zixiang Xu,
  • Yuzeng Li,
  • Xu Liu,
  • Zeyu Wei,
  • Qinran Li,
  • Hongfeng Zhang,
  • Qiliang Deng

摘要

Protein phosphorylation is a common yet critical type of post-translational modification. The selective recognition and enrichment of phosphorylated peptides are essential for the structural identification of phosphorylated proteins and subsequent biomedical research. A method was developed using reversible addition-fragmentation chain transfer (RAFT) polymerization to graft a controllable imprinted polymer layer on the surface, enabling the recognition of phosphorylated angiotensin II (PAngII) via dummy template molecular imprinting technology with phenylphosphonic acid (PPA) as the template. After modifying silica particles with vinyl and disulfide groups, PPA and functional monomers were added to initiate polymerization reactions, forming a controllable polymer layer covalently attached to the silica particle surface. Effective imprinting sites were created through hydrogen bonding between the functional monomer allyl urea and PPA. Under RAFT regulation, the binding capacity for PPA was 0.372 mg g–1 with an imprinting factor (IF) of 2.12, while the binding capacity for PAngII was 0.719 mg g–1 with an IF of 1.86. These IF values were significantly higher than those obtained without RAFT regulation. Additionally, PAngII was recognized by the imprinted particles even in the presence of non-phosphorylated peptides. The recognized performance of PAngII remained at 93% after five cycles of adsorption and desorption. It was demonstrated that surface-grafted, controllable imprinted particles using a dummy template and RAFT strategy show great promise for phosphopeptide recognition, exhibiting good selectivity and reusability.