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Cost-Effective Plasmonic Platforms: Glass Capillaries Decorated with Ag@SiO<sub>2</sub> Nanoparticles on Inner Walls as SERS Substrates

M. ShanthilPhotosciences and Photonics, CSIR-National Institute for Interdisciplinary Science and Technology, Thiruvananthapuram 695 019, IndiaHemna FathimaSchool of Chemistry, Indian Institute of Science Education and Research Thiruvananthapuram (IISER-TVM), CET Campus, Thiruvananthapuram 695 016, IndiaK. George ThomasSchool of Chemistry, Indian Institute of Science Education and Research Thiruvananthapuram (IISER-TVM), CET Campus, Thiruvananthapuram 695 016, India
2017en
ABI

Аннотация

A cost-effective method for the fabrication of a glass capillary based plasmonic platform for the selective detection and identification of analytes of importance in health, environment, and safety is demonstrated. This was achieved by coating Ag@SiO2 nanoparticles (Ag ∼ 60 nm) having silica shell of varying thickness (∼2 and ∼25 nm) on the inside walls of glass capillaries, over 2 cm in length, with uniform coverage. It was found that the particle density on the surface plays a decisive role on the enhancement of Raman signals. Multiple hot spots, which are essentially junctions of amplified electric field, were generated when ∼30 Ag@SiO2 particles/μm2 were bound onto the walls of glass capillaries. The pores of the silica shell allow the localization of analyte molecules to the vicinity of hot spots resulting in signal enhancements of the order of 1010 (using pyrene as analyte; excitation wavelength, 632.8 nm). The applicability of Ag@SiO2 coated capillaries for the detection of a wide range of molecules has been explored, by taking representative examples of polyaromatic hydrocarbons (pyrene), amino acids (tryptophan), proteins (bovine serum albumin), and explosives (trinitrotoluene). By increasing the thickness of the silica shell of Ag@SiO2 nanoparticles, an effective filtration cum detection method has been developed for the selective identification of small molecules such as amino acids, without the interference of large proteins.

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