ABSTRACT
We present a highly efficient structural color filtering approach for large-area application, using a nanoporous anodic alumina (NAA) film overlaid with an aluminum (Al) layer on top of an optically thick Al substrate. The NAA film, consisting of a self-assembled nanopore array in a hexagonal lattice, is equivalent to a quasi-homogeneous medium according to effective medium theory. The proposed structure enables strong absorption at resonance owing to the Fabry-Perot resonance supported by the metal-dielectric-metal configuration and the plasmonic effect mediated by the top nanoporous Al layer. The reflection colors can be readily tuned by altering the NAA thickness that is determined by anodization time, thereby allowing the flexible creation of complicated color images on a single platform. By fabricating three samples with different NAA thicknesses in a large area of 2 cm × 2 cm, it is confirmed that the proposed color filtering scheme exhibits highly enhanced color purity and high reflection efficiency of up to 73%, which is superior to that generated by previously reported NAA-based approaches. The presented strategy can pave the way for the efficient fabrication of large-area color filtering devices for various potential applications, including color display devices, imaging sensors, structural color printing, and photovoltaic cells.
ABSTRACT
OBJECTIVE: To establish the method for studying the proteome of the lens fibers of healthy adult male in order to provide a tool for further analysis of cataract-related protein using reverse tandem mass spectrometry. METHODS: Lens fibers proteins were separated and analyzed using sodium dodecyl sulfate polyacrylamide gel electrophoresis followed by RPLC-MS/MS (SDS-PAGE-RPLC/MS/MS). The experiment was repeated three times. The tandem mass spectra of positive results were quality controlled by SEQUEST/AMASS softwares which were based on high abundance ion matching rate, continuity of matched ions and randomnicity score proteins were identified based on 2-hit criteria with reliability over 98% for each peptide. RESULTS: Total 60 lens fibers proteins were identified at least twice in three experiments. Among these proteins, 22 were identified in previous lens proteome study. CONCLUSION: The results in this study provided preliminary data on the composition of crystallin in the lens fibers of healthy adult male. The results can be used as a reference for future studies to detect the changes of human lens proteins during aging and cataract formation. Combination of SDS-PAGE and RPLC/MS/MS is a quick and simple method, it may be useful for large scale analysis of clinical samples.
