Enzymatic fabrication of protein-decorated gold nanoparticles in Escherichia coli

2014 Fiscal Year Final Research Report

• Project/Area Number: 25630385
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Biofunction/Bioprocess
• Research Institution: Kyushu University
• Principal Investigator: KAMIYA Noriho 九州大学, 工学(系)研究科(研究院), 教授 (50302766)
• Project Period (FY): 2013-04-01 – 2015-03-31
• Keywords: 蛋白質 / 金ナノ粒子 / 生体触媒 / 補酵素 / 酸化還元酵素 / ナノバイオ / イムノクロマト / 抗体

Outline of Final Research Achievements

In the present study, we explored a new approach for the biofabrication of protein-decorated gold nanoparticles (AuNP) by glycerol dehydrogenase (GLD) enzyme with gold-binding peptide-tagged recombinant proteins. The formation of AuNP was achieved via the GLD-catalyzed reduction of NAD to NADH with glycerol as a substrate. In the presence of the fusion protein comprised of protein G (pG) and a gold-binding peptide (GBP), the catalytic cofactor reduction resulted in the efficient in situ fabrication of AuNP immobilized with the fusion protein. Next, we designed a GLD fusion protein tagged with both pG and GBP. The recombinant pG-GLD-GBP protein promoted the synthesis of AuNP, and the pG moiety was self-displayed on the AuNPs with the protein G's binding capability for IgG antibody. Finally, we confirmed that an engineered E. coli harboring the pG-GLD-GBP fusion protein could produce AuNP decorated with functional pG, suggesting the possibility of in vivo fabrication of functional AuNPs.

Free Research Field

生体分子工学