Journal
JOURNAL OF POLYMER SCIENCE PART A-POLYMER CHEMISTRY
Volume 54, Issue 16, Pages 2599-2610Publisher
WILEY
DOI: 10.1002/pola.28138
Keywords
adsorption; biopolymers; fluorinated amphiphilic polymer; phase separation; protein resistance; surface; thin films; V-shaped polymer brush
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Funding
- National Natural Science Foundation of China (NSFC) [21174134, 21374104]
- Natural Science Foundation of Zhejiang Province [LQ16B040001]
- Science Foundation of Education Department of Zhejiang Province [Y201534629]
- Science Foundation of Zhejiang Sci-Tech University [15062020-Y]
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In this article, the fluorinated amphiphilic V-shaped brushes with two highly incompatible arms of mPEG42 and PMMA(38)-b-PFMAy were produced by reacting -COOH in the PAA segment in methoxypoly(ethylene glycol)-b-poly(acrylic acid)-b-poly(methyl methacrylate)-b-poly(2-perfluoro-octylethyl methacrylate) (mPEG(42)-b-PAA(11)-b-PMMA(38)-b-PFMA(y)) with an epoxy group on the functionalized SiO2 substrate. It was found that the resulting phase separation structures of the V-shaped brushes can be adjusted by altering the degree of polymerization (y) of PFMA. The brush surface with y=8 showed an alternating phase separation structure, in which one domain was water-soluble PEG and the other was ultralow surface energy domain with a crystalline fluorinated side group. Protein adsorption studies indicated that this surface structure exhibited desirable protein-resistant performance. The reason was attributed to the stimuli-responsive PEG domain, in which PEG chains stretch out at the interface in water, while the PFMA domain remains relatively stable. The synergistic effect of the hydrophilic PEG domain and the hydrophobic PFMA domain in water prevents protein adsorption. (C) 2016 Wiley Periodicals, Inc.
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