Specific removal of protein using protein imprinted polydopamine shells on modified amino-functionalized magnetic nanoparticles

  • Ruixia Gao
  • , Lili Zhang
  • , Yi Hao
  • , Xihui Cui
  • , Yuhai Tang

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

Abstract

Thin imprinted shells over functionalized magnetic nanoparticles is an effective solution to weaken mass transfer resistance, achieve high binding capacity, and attain rapid separation. In this work, a simple, green, and effective approach was developed to imprint bovine serum albumin (BSA) on the surface of amino-modified Fe3O4 nanoparticles (Fe3O4@NH2) using dopamine as monomer through a two-step immobilized template strategy. The results of X-ray diffraction and vibrating sample magnetometry indicated that the as-synthesized nanomaterials exhibited high crystallinity and satisfactory superparamagnetic properties. Transmission electron microscopy and Fourier transform infrared spectroscopy of the products showed that polydopamine shells successfully attached onto Fe3O4@NH2. The polydopamine shells with a thickness of about 10 nm enable the template recognition sites to be accessed easily, and exhibit fast kinetics and high adsorption capacity in aqueous solution. Meanwhile, an excellent selectivity towards BSA has been presented when bovine hemoglobin (BHb), transferrin, and immunoglobulin G (IgG) were employed as competitive proteins. Good recovery after a reasonably mild elution and successful capture of the target protein from a real sample of bovine blood suggests its potential value in practical applications. In addition, the resultant polymers were stable and had no obvious deterioration after six adsorption-regeneration cycles. The versatility of the proposed method has also been verified by choosing four other proteins with different isoelectric points as the templates.

Original languageEnglish
Pages (from-to)64514-64524
Number of pages11
JournalRSC Advances
Volume4
Issue number110
DOIs
StatePublished - 2014

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