| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1234424 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2012 | 6 Pages |
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.
Graphical abstractFigure optionsDownload full-size imageDownload 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.
