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

Yaşar M., Dal Y., Kahraman M. V., Kayaman A., Aktaş Z., Öncül M., ...Daha Fazla

JOURNAL OF BIOMATERIALS SCIENCE-POLYMER EDITION, cilt.31, ss.2044-2059, 2020 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 31
  • Basım Tarihi: 2020
  • Doi Numarası: 10.1080/09205063.2020.1793705
  • Dergi Adı: JOURNAL OF BIOMATERIALS SCIENCE-POLYMER EDITION
  • Derginin Tarandığı İndeksler: 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
  • Sayfa Sayıları: ss.2044-2059
  • Anahtar Kelimeler: Molecularly imprinted polymer, thiol-ene polymerization, photopolymerization, myoglobin, plastic antibody, SOLID-PHASE EXTRACTION, IMPRINTED POLYMERS, PERFORMANCE, SEPARATION, LYSOZYME
  • Marmara Üniversitesi Adresli: Evet

Özet

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.