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    Hydrophilic modification of polystyrene with hydrophobin for time-resolved immunofluorometric assay

    Year: 2010

    Journal: Biosensors and Bioelectronics, Volume 26, Issue 3, 15 November 2010, Pages 1074-1079, 20101201

    Authors: Wang Z. 1 3, Huang Y. 1, Li S. 2, Xu H. 2, Linder M.B. 3, Qiao M. 1

    Last authors: Mingqiang Qiao

    Organizations: 1 The Key Laboratory of Bioactive Materials, Ministry of Education, College of Life Sciences, Nankai University, No. 94 Weijin Road, Tianjin 300071, PR China 2 The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, No. 94 Weijin Road, Tianjin 300071, PR China 3 VTT Biotechnology, Technical Research Centre of Finland, Finland

    Country: China

    Herein we reported that a hydrophobin film was used as a solid support on the polystyrene surface for immobilizing antibodies in the time-resolved immunofluorometric assay (TR-IFMA). Quartz crystal microbalance with dissipative monitoring (QCM -D), X-ray photoelectron spectroscopy (XPS) and water contact angle (WCA) measurements, as well as atomic force microscope (AFM) were used to characterize the hydrophilic modification of polystyrene surface with Class I hydrophobin isolated from Grifola frondosa (HGFI). The performance of HGFI-modified polystyrene was evaluated by TR-IFMA of carcinoembryonic antigen (CEA). QCM -D revealed that HGFI formed an intact monolayer on the polystyrene at pH 5. XPS and WCA measurements showed that self-assembling HGFI could render polystyrene surface hydrophilic for three months. AFM indicated that an end-on antibody monolayer was adsorbed on the HGFI film rather than multilayers on the polystyrene in a side-on orientation. Furthermore, a linear calibration curve (from 5 to 600 ng/mL) of CEA showed HGFI-modified polystyrene had higher detection sensitivity than unmodified ones in TR-IFMA. This present method for modifying polystyrene is simple without severe chemical treatment and may have wide applicability to functionalize other supports for immobilizing biomolecules.