Biocatalytic Formation of Gold Nanoparticles Decorated with Functional Proteins inside Recombinant Escherichia coli Cells

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  • HOSOMOMI Yukiho
    Department of Applied Chemistry, Graduate School of Engineering, Kyushu University
  • NIIDE Teppei
    Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
  • WAKABAYASHI Rie
    Department of Applied Chemistry, Graduate School of Engineering, Kyushu University
  • GOTO Masahiro
    Department of Applied Chemistry, Graduate School of Engineering, Kyushu University Center for Future Chemistry, Kyushu University
  • KAMIYA Noriho
    Department of Applied Chemistry, Graduate School of Engineering, Kyushu University Center for Future Chemistry, Kyushu University

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タイトル別名
  • Biocatalytic Formation of Gold Nanoparticles Decorated with Functional Proteins inside Recombinant <i>Escherichia coli</i> Cells

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抄録

A novel strategy for the preparation of protein-decorated gold nanoparticles (Au NPs) was developed inside Escherichia coli cells, where an artificial oxidoreductase, composed of antibody-binding protein (pG), Bacillus stearothermophilus glycerol dehydrogenase (BsGLD) and a peptide tag with gold-binding affinity (H6C), was overexpressed in the cytoplasm. In situ formation of Au NPs was promoted by a natural electron-donating cofactor, nicotinamide adenine dinucleotide (NAD), which was regenerated to the reduced form of NADH by the catalytic activity of the fusion protein (pG-BsGLD-H6C) overexpressed in the cytoplasm of E. coli, with the concomitant addition of exogenous glycerol to the reaction system. The fusion protein was self-immobilized on Au NPs inside the E. coli cells, which was confirmed by SDS-PAGE and western blotting analyses of the resultant Au NPs. Finally, the IgG binding ability of the pG moiety displayed on Au NPs was evaluated by an enzyme-linked immunosorbent assay.

収録刊行物

  • Analytical Sciences

    Analytical Sciences 32 (3), 295-300, 2016

    社団法人 日本分析化学会

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