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Abstract
An enzymatic reaction was employed as a means to enhance the sensitivity of an immunosensor based on localized surface plasmon resonance (LSPR). The reaction occurs after intermolecular binding between an antigen and an antibody on gold nano-island (NI) surfaces. For LSPR sensing, the gold NI surface was fabricated on glass substrates using vacuum evaporation and heat treatment. The interferon-γ (IFN-γ) capture antibody was immobilized on the gold NIs, followed by binding of IFN-γ to the antibody. Subsequently, a biotinylated antibody and a horseradish peroxidase (HRP) conjugated with avidin were simultaneously introduced. A solution of 4-chloro-1-naphthol (4-CN) was then used for precipitation; precipitation was the result of the enzymatic reaction catalyzed the HRP on gold NIs. The LSPR spectra were obtained after each binding process. Using this method, the enzyme-catalyzed precipitation reaction on the gold NI surface was found to effectively amplify the change in the signal of the LSPR immunosensor after intermolecular binding.
Highlights
Studies on the detection of biomolecules using localized surface plasmon resonance (LSPR) have been recently accelerated by the development of various nanostructure fabrication techniques
We demonstrated a novel approach in which enzyme-catalyzed precipitation was induced on the gold nano-island (NI) surface after binding between interferon- (IFN- ) and an IFN- antibody to enhance the sensitivity of detection based on LSPR analysis of gold NIs
Thin gold films (t < 10 nm) that are deposited slowly (
Summary
Studies on the detection of biomolecules using localized surface plasmon resonance (LSPR) have been recently accelerated by the development of various nanostructure fabrication techniques. We have developed a novel approach for the detection of biomolecules, in which LSPR optical detection with gold NI was implemented to analyze binding of proteins to surfaces functionalized with the corresponding high affinity ligands. This method was used to rapidly detect recombinant GST-tagged hIL6 expressed in Escherichia coli by attenuated total reflection (ATR). When large molecules, such as proteins, are used as the receptors, the sensitivity in detecting binding events with LSPR is expected to be conspicuously lower This is expected since the penetration depth of the LSP field in metal 3-D nanostructures is a few tens of nanometers at most [6,7,8]. We demonstrated a novel approach in which enzyme-catalyzed precipitation was induced on the gold nano-island (NI) surface after binding between interferon- (IFN- ) and an IFN- antibody to enhance the sensitivity of detection based on LSPR analysis of gold NIs
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