Selective Binding of Inhibitor-Assisted Surface-Imprinted Core/Shell Microbeads in Protein Mixtures

Dinc M., BASAN H., Hummel T., Mueller M., Sobek H., Rapp I., ...More

CHEMISTRYSELECT, vol.3, no.16, pp.4277-4282, 2018 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 3 Issue: 16
  • Publication Date: 2018
  • Doi Number: 10.1002/slct.201800129
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.4277-4282
  • Keywords: Surface chemistry, Molecular recognition, Core-shell microbeads, Inhibitor-assisted, Protein imprinting, POLYMERS, RECOGNITION, ANTIBODIES, RECEPTORS, PEPSIN
  • Gazi University Affiliated: Yes


An innovative approach for molecularly imprinting proteins, i.e., inhibitor-assisted imprinting was used for addressing the major challenge of protein purification from biotechnologically relevant media. Pepstatin-assisted pepsin surface-imprinted microbeads were synthesized as a selective sorbent for solid phase extraction (SPE). The amino-functionalized porous core was prepared by co-condensation and post-grafting strategies. The immobilized inhibitor pre-organizes the template pepsin with a defined orientation prior to imprinting ensuring enhanced efficiency of the imprinting process. 3-aminophenylboronic acid (APBA) was used as a functional monomer establishing organic nanoscale films comprising poly(3-aminophenylboronic acid) (pAPBA) within the pores of the beads in the presence (MIP) and absence (NIP) of pepsin. Next to a detailed characterization of these advanced functional hybrid materials it was demonstrated that such porous surface-imprinted core/shell beads feature exquisite selectivity for pepsin during individual protein rebinding studies, and more importantly, during competitive rebinding studies in protein mixtures.