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Protein-inorganic hybrid nanoflowers
Alternative TitleNat. Nanotechnol.
Ge, Jun1,3; Lei, Jiandu2,3; Zare, Richard N.3
2012-07-01
Source PublicationNATURE NANOTECHNOLOGY
ISSN1748-3387
Volume7Issue:7Pages:428-432
AbstractFlower-shaped inorganic nanocrystals(1-3) have been used for applications in catalysis(4,5) and analytical science(6,7), but so far there have been no reports of 'nanoflowers' made of organic components(8). Here, we report a method for creating hybrid organic-inorganic nanoflowers using copper (II) ions as the inorganic component and various proteins as the organic component. The protein molecules form complexes with the copper ions, and these complexes become nucleation sites for primary crystals of copper phosphate. Interaction between the protein and copper ions then leads to the growth of micrometre-sized particles that have nanoscale features and that are shaped like flower petals. When an enzyme is used as the protein component of the hybrid nanoflower, it exhibits enhanced enzymatic activity and stability compared with the free enzyme. This is attributed to the high surface area and confinement of the enzymes in the nanoflowers.; Flower-shaped inorganic nanocrystals(1-3) have been used for applications in catalysis(4,5) and analytical science(6,7), but so far there have been no reports of 'nanoflowers' made of organic components(8). Here, we report a method for creating hybrid organic-inorganic nanoflowers using copper (II) ions as the inorganic component and various proteins as the organic component. The protein molecules form complexes with the copper ions, and these complexes become nucleation sites for primary crystals of copper phosphate. Interaction between the protein and copper ions then leads to the growth of micrometre-sized particles that have nanoscale features and that are shaped like flower petals. When an enzyme is used as the protein component of the hybrid nanoflower, it exhibits enhanced enzymatic activity and stability compared with the free enzyme. This is attributed to the high surface area and confinement of the enzymes in the nanoflowers.
KeywordSingle-enzyme Metal-ions Nanogel Immobilization Nanostructures Nanodendrites Resolution Support Binding Laccase
SubtypeArticle
WOS HeadingsScience & Technology ; Technology
DOI10.1038/NNANO.2012.80
URL查看原文
Indexed BySCI
Language英语
WOS KeywordSINGLE-ENZYME ; METAL-IONS ; NANOGEL ; IMMOBILIZATION ; NANOSTRUCTURES ; NANODENDRITES ; RESOLUTION ; SUPPORT ; BINDING ; LACCASE
WOS Research AreaScience & Technology - Other Topics ; Materials Science
WOS SubjectNanoscience & Nanotechnology ; Materials Science, Multidisciplinary
WOS IDWOS:000306112000008
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Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/6460
Collection研究所(批量导入)
Affiliation1.Tsinghua Univ, Dept Chem Engn, Beijing 100084, Peoples R China
2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
3.Stanford Univ, Dept Chem, Stanford, CA 94305 USA
Recommended Citation
GB/T 7714
Ge, Jun,Lei, Jiandu,Zare, Richard N.. Protein-inorganic hybrid nanoflowers[J]. NATURE NANOTECHNOLOGY,2012,7(7):428-432.
APA Ge, Jun,Lei, Jiandu,&Zare, Richard N..(2012).Protein-inorganic hybrid nanoflowers.NATURE NANOTECHNOLOGY,7(7),428-432.
MLA Ge, Jun,et al."Protein-inorganic hybrid nanoflowers".NATURE NANOTECHNOLOGY 7.7(2012):428-432.
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