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Self-Assembling Protein–Polymer Bioconjugates for Surfaces with Antifouling Features and Low Nonspecific Binding
Author(s) -
Yingying Liu,
Tarja K. Nevanen,
Arja Paananen,
Kristian Kempe,
Paul Wilson,
LeenaSisko Johansson,
Jussi J. Joensuu,
Markus B. Linder,
David M. Haddleton,
Roberto Milani
Publication year - 2018
Publication title -
acs applied materials and interfaces
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.535
H-Index - 228
eISSN - 1944-8252
pISSN - 1944-8244
DOI - 10.1021/acsami.8b19968
Subject(s) - biofouling , protein adsorption , contact angle , hydrophobin , materials science , polymerization , ethylene glycol , monolayer , adsorption , surface modification , polymer , acrylate , chemical engineering , polymer chemistry , radical polymerization , raft , covalent bond , organic chemistry , chemistry , nanotechnology , membrane , copolymer , biochemistry , engineering , composite material , gene
A new method is demonstrated for preparing antifouling and low nonspecific adsorption surfaces on poorly reactive hydrophobic substrates, without the need for energy-intensive or environmentally aggressive pretreatments. The surface-active protein hydrophobin was covalently modified with a controlled radical polymerization initiator and allowed to self-assemble as a monolayer on hydrophobic surfaces, followed by the preparation of antifouling surfaces by Cu(0)-mediated living radical polymerization of poly(ethylene glycol) methyl ether acrylate (PEGA) performed in situ. By taking advantage of hydrophobins to achieve at the same time the immobilization of protein A, this approach allowed to prepare surfaces for IgG1 binding featuring greatly reduced nonspecific adsorption. The success of the surface modification strategy was investigated by contact angle, XPS, and AFM characterization, while the antifouling performance and the reduction of nonspecific binding were confirmed by QCM-D measurements.

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