Glycopolymer brushes with specific protein recognition property

Kursun T. T., Cimen D., ÇAYKARA T.

JOURNAL OF APPLIED POLYMER SCIENCE, cilt.134, sa.36, 2017 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 134 Sayı: 36
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1002/app.45238
  • Dergi Adı: JOURNAL OF APPLIED POLYMER SCIENCE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: glycopolymer brushes, pentafluorophenyl acrylate, specific protein recognition, TRANSFER RADICAL POLYMERIZATION, WELL-DEFINED GLYCOPOLYMER, CONCANAVALIN-A, SWEET SPOT, SURFACE, GLYCOBIOLOGY, BINDING, MONOLAYERS, DESIGN, THIOL
  • Gazi Üniversitesi Adresli: Evet

Özet

Here, we report the synthesis of glycopolymer brushes on the silicon substrate by interface-mediated reversible addition-fragmentation chain transfer polymerization of pentafluorophenyl acrylate as well as subsequent attachment of d-glucosamine to determine specific and nonspecific protein interactions. The root-mean-square roughness of the glycopolymer brushes is only about 3.1 nm, indicating unstable distribution of the collapsed glycopolymer chains on the surface. The water contact angle of glycopolymer brush was determined as approximate to 53 degrees indicating a hydrophilic behavior. The results of fluorescence microscopy studies indicated that the glycopolymer brushes have specific interaction with fluorescence-labeled Concanavalin A and nonspecific interaction with fluorescence-labeled bovine serum albumin. The glycopolymer brushes tested here are hoped to enlarge to our knowledge of recognition phenomena at the surface of polymer brushes. (c) 2017 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2017, 134, 45238.