Recycling protein selective adsorption on fluorine-modified surface through fluorine-fluorine interaction

Low surface energy materials with micro-nano structures have been widely developed to prevent non-specific adhesion of biomolecules. Herein we put forward a new approach based on the antifouling and self-assembly properties of fluorine components, to construct a non-specific protein resistance surface with selective protein adsorption property. Briefly, the antifouling surface (SN-F) was obtained by a simple one-step modification on silicon nanowire arrays (SiNWAs) with fluorine coupling agent 1 H,1 H,2 H,2 H-perfluorodecyltrimethoxysilane (FAS). And protein was fluorinated by conjugation with an amphiphilic fluoro-copolymer, produced from 2-methacrylamido glucopyranose (MAG) and trifluoroethyl methacrylate (TFEMA) via RAFT polymerization. The properties of the materials were characterized by ¹H nuclear magnetic resonance (¹H NMR), infrared spectroscopy (FTIR), water contact angle, and X-ray photoelectron spectroscopy (XPS) etc., and protein adsorption was investigated by protein content measurement, fluorescence detection, and electrophoresis. It was observed that the adsorption for native proteins on SN-F was at an extremely low level, while the adsorption for the fluoro-copolymer conjugated protein (PFG-BSA) was significantly increased. When the percentage of TFEMA in the fluoro-copolymer was as high as 52.0%, the fluorinated protein adsorbed on SN-F was more than 35 times of native proteins on the surface. Moreover, the platform could resist IgG adhesion in serum after the adsorption of fluorinated protein, and it could be recycled three times after 75% ethanol treatment. In conclusion, SN-F showed non-specific protein resistance through low surface energy and specific protein adsorption by fluorine-fluorine self-assembly. The fluorinated nanostructured platform has a great potential in controlling protein adsorption and release.