A novel route to prepare a multilayer system via the combination of interface-mediated catalytic chain transfer polymerization and thiol-ene click chemistry

Zengin A., Caykara T.

MATERIALS SCIENCE & ENGINEERING C-MATERIALS FOR BIOLOGICAL APPLICATIONS, vol.74, pp.103-109, 2017 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 74
  • Publication Date: 2017
  • Doi Number: 10.1016/j.msec.2017.02.011
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.103-109
  • Keywords: Surface-mediated catalytic chain transfer polymerization, Thiol-ene click chemistry, Poly(methyl methacrylate) brushes, Anti-immunoglobulin G, IMMUNOGLOBULIN-G, PROTEIN-A, ORIENTED IMMOBILIZATION, MOLECULAR-WEIGHT, SURFACE, BRUSHES, GOLD, ORIENTATION, RECOGNITION, TEMPERATURE
  • Van Yüzüncü Yıl University Affiliated: Yes


Herein, we have designed a novel multilayer system composed of poly(methyl methacrylate) [poly(MMA)] brush, biotin, streptavidin and protein-A on a silicon substrate to attach on anti-immunoglobulin G (anti-IgG). poly(MMA) brush with vinyl end-group was first synthesized by the interface-mediated catalytic chain transfer polymerization. The brush was then modified with cysteamine molecules to generate the polymer chains with amine end-group via a thiol-ene click chemistry. The amine end-groups of poly(MMA) chains were also modified with biotin units to ensure selective connection points for streptavidin molecules. Finally, a multilayer system on the silicon substrate was formed by using streptavidin and protein-A molecules, respectively. This multilayer system was employed to attach anti-IgG molecules in a highly oriented manner and provide anti-IgG molecular functional configuration on the multilayer. High reproducibility of the amount of anti-IgG adsorption and homogeneous anti-IgG adsorption layer on the silicon surface could be provided by this multilayer system. The multi layer system with protein A may be opened the door for designing an efficient immunoassay protein chip. (C) 2017 Published by Elsevier B.V.