Self-Assembly of Ferritin Nanoparticles into an Enzyme Nanocomposite with Tunable Size for Ultrasensitive Immunoassay
| Autor: | Xian-En Zhang, Jiao-Yu Deng, Ting-Ting Zhang, Jin-Li Zhang, Yuan-Yuan Shi, Dianbing Wang, Zongqiang Cui, Li-Wei Hou, Zhiping Zhang, Dong Men, Juan Zhou |
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| Rok vydání: | 2015 |
| Předmět: |
Streptavidin
Materials science General Physics and Astronomy Nanoparticle Nanotechnology Enzyme-Linked Immunosorbent Assay Horseradish peroxidase Nanomaterials Nanocomposites chemistry.chemical_compound Humans General Materials Science Biotinylation Particle Size Horseradish Peroxidase Immunoassay Nanocomposite biology Staining and Labeling Troponin I General Engineering Recombinant Proteins chemistry Ferritins biology.protein Nanoparticles Self-assembly Particle size |
| Zdroj: | ACS nano. 9(11) |
| ISSN: | 1936-086X |
| Popis: | The self-assembly of nanoparticles into larger superstructures is a powerful strategy to develop novel functional nanomaterials, as these superstructures display collective properties that are different to those displayed by individual nanoparticles or bulk samples. However, there are increasing bottlenecks in terms of size control and multifunctionalization of nanoparticle assemblies. In this study, we developed a self-assembly strategy for construction of multifunctional nanoparticle assemblies of tunable size, through rational regulation of the number of self-assembling interaction sites on each nanoparticle. As proof-of-principle, a size-controlled enzyme nanocomposite (ENC) was constructed by self-assembly of streptavidin-labeled horseradish peroxidase (SA-HRP) and autobiotinylated ferritin nanoparticles (bFNP). Our ENC integrates a large number of enzyme molecules, together with a streptavidin-coated surface, allowing for a drastic increase in enzymatic signal when the SA is bound to a biotinylated target molecule. As result, a 10 000-fold increase in sensitivity over conventional enzyme-linked immunosorbent assays (ELISA) methods was achieved in a cardiac troponin immunoassay. Our method presented here should provide a feasible approach for constructing elaborate multifunctional superstructures of tunable size useful for a broad range of biomedical applications. |
| Databáze: | OpenAIRE |
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