RESUMO
Herein, a novel colorless anti-counterfeiting luminous ink composite material, to the best of our knowledge, was prepared by incorporating upconverted persistent luminescent Zn3Ga2SnO8:1%Cr3+, 5%Yb3+, 0.5%Er3+ (ZGSO: Cr,Yb,Er) phosphors into a resin solution, followed by stirring. Owing to its small particle size and uniform distribution, ZGSO: Cr, Yb, Er exhibits long-lasting, persistent near-infrared emission at 696 nm following the stoppage of excitation by a 274 nm ultraviolet light and a 980 nm excitation. ZGSO: Cr, Yb, Er composites were prepared and exhibited characteristic peaks corresponding to upconversion and an afterglow curve following excitation at 980 nm. With various special luminescent modes, sharp emission peaks, and emission intensity varying over time, the emission light of composite ink is easy to detect and not easily confused. Furthermore, the prepared composite ink can be calligraphic, visualized, and observable, and has good light-emitting performance following UV excitation. Our work provides a meaningful way to fabricate multifunctional anti-counterfeiting luminous ink composites with an intense persistent luminescence for use in anti-counterfeiting signs, inspection imaging, and other complex industrial applications.
RESUMO
Influenza virus still poses a major threat to human health worldwide. The nucleoprotein (NP) of influenza A virus plays an essential role in the viral replication and transcription and hence becomes a promising therapeutic target. NP forms a complicated conformation under native conditions and might denature when performing immunoassays such as western blot in the study of NP function. Therefore, it is useful to make an NP specific monoclonal antibody (mAb) that recognizes linear epitope instead of conformational epitope. In this study, a recombinant NP (rNP) of influenza A virus was over-expressed and used to generate a panel of anti-NP mAbs. These anti-NP mAbs were grouped into three classes based on their reactivity in Western blots. Only Class I mAb can react with linear rNP fragments. One of Class I mAb, 4D2, was characterized further by epitope mapping with a series of overlapping synthetic peptides, indicating that the 4D2 epitope is a surface exposed, linear epitope between amino acid residues 243 and 251. This epitope is highly conserved among different influenza A viruses with an identity of 98.4% (17,922/18,210). Western blot, co-immunoprecipitation, immunofluorescence, and immunohistochemistry experiments all indicated 4D2 is highly specific to NP of influenza A virus. The results demonstrated that 4D2 can be used as a research tool for functional study of NP in the replication cycle of influenza A virus. Further work is needed to understand the function and importance of this epitope.
