Biocatalytic formation of gold nanoparticles decorated with functional proteins inside recombinant Escherichia coli cells

Yukiho Hosomomi, Teppei Niide, Rie Wakabayashi, Masahiro Goto, Noriho Kamiya

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

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 (H 6 C), 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-BsGLDH 6 C) 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. 2016

Original languageEnglish
Pages (from-to)295-300
Number of pages6
Journalanalytical sciences
Volume32
Issue number3
DOIs
Publication statusPublished - Jan 1 2016

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Recombinant Proteins
Gold
Escherichia coli
glycerol dehydrogenase
Nanoparticles
NAD
Fusion reactions
Immunosorbents
Proteins
Bacilli
Glycerol
Assays
Catalyst activity
Carrier Proteins
Oxidoreductases
Immunoglobulin G
Peptides
Electrons
Antibodies
Enzymes

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry

Cite this

Biocatalytic formation of gold nanoparticles decorated with functional proteins inside recombinant Escherichia coli cells. / Hosomomi, Yukiho; Niide, Teppei; Wakabayashi, Rie; Goto, Masahiro; Kamiya, Noriho.

In: analytical sciences, Vol. 32, No. 3, 01.01.2016, p. 295-300.

Research output: Contribution to journalArticle

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