Hydrophobins are a type be used to modify material surfaces of small amphipathic proteins with a and adsorb enzymes, antibodies and unique self-assembly property, which can even cells. In this study, a fusion protein ...Hydrophobins are a type be used to modify material surfaces of small amphipathic proteins with a and adsorb enzymes, antibodies and unique self-assembly property, which can even cells. In this study, a fusion protein consisting of hydrophobin HGFI and green fluorescent protein（GFP） was successfully obtained from Pichia patoris （P. pastoris）. Water contact angle（WCA） measurement proves that the wettability of the surfaces of different materials was changed. We further demonstrated the self-assembly ability of HGFI-GFP, which can be used to disperse the multi-walled carbon nanotubes（MWCNTs）. Finally, the adsorption of HGFI-GFP onto the surface of the tissue engineering material poly（ε-caprolactone）（PCL） was evaluated by detecting the fluorescence of the fusion protein itself. The resalt demonstrates that both the basic self-assembly activity of the HGFI domain and the functional activity of the GFP domain were still remained.展开更多
基金Supported by the National Natural Science Foundation of China（No.31170066） and the Tianjin Key Research Program of Application Foundation and Advanced Technology, China（No. 12JCZDJC22600）.
文摘Hydrophobins are a type be used to modify material surfaces of small amphipathic proteins with a and adsorb enzymes, antibodies and unique self-assembly property, which can even cells. In this study, a fusion protein consisting of hydrophobin HGFI and green fluorescent protein（GFP） was successfully obtained from Pichia patoris （P. pastoris）. Water contact angle（WCA） measurement proves that the wettability of the surfaces of different materials was changed. We further demonstrated the self-assembly ability of HGFI-GFP, which can be used to disperse the multi-walled carbon nanotubes（MWCNTs）. Finally, the adsorption of HGFI-GFP onto the surface of the tissue engineering material poly（ε-caprolactone）（PCL） was evaluated by detecting the fluorescence of the fusion protein itself. The resalt demonstrates that both the basic self-assembly activity of the HGFI domain and the functional activity of the GFP domain were still remained.
