کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1234424 | 1495272 | 2012 | 6 صفحه PDF | دانلود رایگان |
By the aim of constructing surfaces for multi-component and multifunctional bioassay, a microsphere lithography technique was employed to control the surface morphology. Two kinds of protein molecules (antibodies) were used as building blocks. As a result, dual-component biocompatible surfaces with alternate immunoglobulin micropatterns were fabricated. The employed antibodies included human Immunoglobulin G (IgG) and rabbit IgG, which composed nanometer scale surface arrays on the surfaces. The antibodies were identified specially by immunoreactions with labeled antigens of fluorescein isothiocyanate (FITC)-antihuman IgG and tetramethylrhodamine-5-(and 6)-isothiocyanate (TRITC)-antirabbit IgG. The immune responses were confirmed by confocal fluorescence (FL) microscopy. A study on the sensitivity and quantification was done by using surface-enhanced resonance Raman scattering (SERRS) spectroscopy. The obtained SERRS spectra showed satisfactory resolution in the multi-component detection objects. No interference was observed from inner- or interactions of detecting molecules. The detection limits for both of the antigens reached to as low as 1 ng/mL, which was comparable to FL method. Meanwhile, a good linear relationship between SERRS peak intensity and the logarithm of antigens’ concentrations (from 1 ng/mL to 1 mg/mL) were observed. The results demonstrated that SERRS is a very promising detection technique for multi-component immunoassay, and has great potential applications in biotechnology and biochemistry.
Figure optionsDownload as PowerPoint slideHighlights
► The samples with shape protein patterns are similar to natural biomolecules.
► Samples have alternative regions which contained separate antibodies.
► Both SERRS spectra of two kinds biomolecules can be obtained simultaneously.
► Relationship of SERRS intensity and proteins are found.
Journal: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy - Volume 96, October 2012, Pages 395–400