Chemical Research in Chinese Universities ›› 2015, Vol. 31 ›› Issue (5): 781-786.doi: 10.1007/s40242-015-5135-x

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A Visualized Fusion Protein Based on Self-assembly Hydrophobin HGFI

ZHAO Liqiang, LIU Jinyuan, SONG Dongmin, WANG Xiangxiang, TAI Feifei, XU Haijin, QIAO Mingqiang   

  1. Key Laboratory of Bioactive Materials, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, P. R. China
  • Received:2015-04-03 Revised:2015-07-15 Online:2015-10-01 Published:2015-07-27
  • Contact: QIAO Mingqiang, E-mail: qiaomq@nankai.edu.cn E-mail:qiaomq@nankai.edu.cn
  • Supported by:

    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).

Abstract:

Hydrophobins are a type of small amphipathic proteins with a unique self-assembly property, which can be used to modify material surfaces and adsorb enzymes, antibodies and 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.

Key words: Self-assembly, Hydrophobin, Fusion protein, Dispersion, Modification