Polymeric nanoparticles for selective protein recognition by using thiol-ene miniemulsion photopolymerization

Yasar M., Dal Yontem F., KAHRAMAN M. V., KAYAMAN APOHAN N., Aktas Z., Oncul M. O., ...More

JOURNAL OF BIOMATERIALS SCIENCE-POLYMER EDITION, vol.31, no.16, pp.2044-2059, 2020 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 31 Issue: 16
  • Publication Date: 2020
  • Doi Number: 10.1080/09205063.2020.1793705
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aerospace Database, BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Communication Abstracts, Compendex, EMBASE, INSPEC, MEDLINE, Metadex, Veterinary Science Database, Civil Engineering Abstracts
  • Page Numbers: pp.2044-2059
  • Keywords: Molecularly imprinted polymer, thiol-ene polymerization, photopolymerization, myoglobin, plastic antibody, SOLID-PHASE EXTRACTION, IMPRINTED POLYMERS, PERFORMANCE, SEPARATION, LYSOZYME
  • Istanbul University Affiliated: Yes


The fabrication of molecularly imprinted nanoparticles (MIP-NPs) specific for myoglobin by using thiol-ene photopolymerization in miniemulsion was described. Allyl derivatives of phenylalanine as a functional monomer was synthesized and copolymerized with acrylic monomersviaminiemulsion polymerization to produce NIP-NPs with approximately 74 nm number average particle diameter. FTIR and(1)H-NMR analysis confirmed the synthesis of functional monomer. MIP-NPs were prepared in the existence of myoglobin as a template protein. Morphological investigations exhibited that the particle size of the MIP-NPs, increased compared to the corresponding NIPs and the mean particle diameter by number was measured as 141 nm with narrow distribution. NIP-NPs that were polymerized without myoglobin were found to have less affinity to the target protein. In addition, the rebinding ability of MIP-NPs was much bigger than that of the corresponding NIPs. ELISA results showed that MIPs interact particularly with the myoglobin and show little affinity for BSA in competitive binding experiments.