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Fundamental research on the label-free detection of protein adsorption using near-infrared light-responsive plasmonic metal nanoshell arrays with controlled nanogap
In this work, we focused on the label-free detection of simple protein binding using near-infrared light-responsive plasmonic nanoshell arrays with a controlled interparticle distance. The nanoshell arrays were fabricated by a combination of colloidal self-assembly and subsequent isotropic helium pl...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3848557/ https://www.ncbi.nlm.nih.gov/pubmed/23758903 http://dx.doi.org/10.1186/1556-276X-8-274 |
Sumario: | In this work, we focused on the label-free detection of simple protein binding using near-infrared light-responsive plasmonic nanoshell arrays with a controlled interparticle distance. The nanoshell arrays were fabricated by a combination of colloidal self-assembly and subsequent isotropic helium plasma etching under atmospheric pressure. The diameter, interparticle distance, and shape of nanoshells can be tuned with nanometric accuracy by changing the experimental conditions. The Au, Ag, and Cu nanoshell arrays, having a 240-nm diameter (inner, 200-nm polystyrene (PS) core; outer, 20-nm metal shell) and an 80-nm gap distance, exhibited a well-defined localized surface plasmon resonance (LSPR) peak at the near-infrared region. PS@Au nanoshell arrays showed a 55-nm red shift of the maximum LSPR wavelength of 885 nm after being exposed to a solution of bovine serum albumin (BSA) proteins for 18 h. On the other hand, in the case of Cu nanoshell arrays before/after incubation to the BSA solution, we found a 30-nm peak shifting. We could evaluate the difference in LSPR sensing performance by changing the metal materials. |
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