Enzymatic fabrication of protein-decorated gold nanoparticles in Escherichia coli
| Project/Area Number |
25630385
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biofunction/Bioprocess
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| Research Institution | Kyushu University |
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Principal Investigator |
KAMIYA Noriho 九州大学, 工学(系)研究科(研究院), 教授 (50302766)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| 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 |
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| 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.
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Report
(3 results)
Research Products
(15 results)
