Surface molecularly imprinted magnetic microspheres for the recognition of albumin


Kartal F., DENİZLİ A.

JOURNAL OF SEPARATION SCIENCE, cilt.37, sa.15, ss.2077-2086, 2014 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 37 Sayı: 15
  • Basım Tarihi: 2014
  • Doi Numarası: 10.1002/jssc.201400086
  • Dergi Adı: JOURNAL OF SEPARATION SCIENCE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.2077-2086
  • Hacettepe Üniversitesi Adresli: Evet

Özet

A new approach, combining metal coordination with the molecular imprinting technique, was developed to prepare affinity materials. Magnetic poly(glycidyl methacrylate) microspheres in monosize form were used for specific recognition toward the target protein. The magnetic poly(glycidyl methacrylate) microspheres were prepared by dispersion polymerization in the presence of magnetite nanopowder. Surface imprinted magnetic poly(glycidyl methacrylate) microspheres based on metal coordination were prepared and used for the selective recognition of human serum albumin. Iminodiacetic acid was used as the metal coordinating agent and human serum albumin was anchored by Cu2+ ions on the surface of magnetic poly(glycidyl methacrylate) microspheres by metal coordination. The magnetic poly(glycidyl methacrylate) microspheres were coated with a polymer formed by condensation of tetraethyl orthosilicate and 3-aminopropyltrimethoxysilane. The human serum albumin imprinted magnetic poly(glycidyl methacrylate) microspheres were characterized by scanning electron microscopy, attenuated total reflectance Fourier transform infrared spectroscopy and particle size analysis. The maximum adsorption capacity of human serum albumin imprinted magnetic poly(glycidyl methacrylate) microspheres was 37.7 mg/g polymer at pH 6.0. The selectivity experiments of human serum albumin imprinted magnetic poly(glycidylmethacrylate) microspheres prepared with different concentrations in the presence of lysozyme, bovine serum albumin and cytochrome C were performed in order to determine the relative selectivity coefficients.