A simple fabrication technique was developed for preparing a mechanically robust superamphiphobic surface on an aluminum (Al) plate. Dual geometric architectures with micro- and nanoscale structures were formed on the surface of the Al plate by a combination of simple chemical etching and anodization. This proposed methodology involves (1) fabrication of irregular microscale plateaus on the surface of the Al plate, (2) formation of nanopores, and (3) fluorination. Wettability measurements indicated that the fabricated Al surface became super-repellent toward a broad range of liquids with surface tension in the range 27.5-72 mN/m. By varying the anodization time, we measured and compared the effects of morphological change on the wettability. The adhesion property and mechanical durability of the fabricated superamphiphobic Al surface were evaluated by the Scotch tape and hardness tests, respectively. The results showed that the fabricated Al surface retained mechanical robustness because the down-directed surface made by nanopores on the microtextured surface was durable enough even after high force was applied. Almost no damage of the film was observed, and the surface still exhibited superamphiphobicity after the tests. The fabricated superamphiphobic surface also remained stable after long-term storage. The simple and time-saving fabrication technique can be extended to any large-area three-dimensional surface, making it potentially suitable for large-scale industrial fabrications of mechanically robust superamphiphobic surfaces.

Ginsenosides, dammarane-type triterpene saponins obtained from ginseng, have been used as a natural medicine for many years in the Orient due to their various pharmacological activities. However, the therapeutic potential of ginsenosides has been largely limited by the low bioavailability of the natural products caused mainly by low aqueous solubility, poor biomembrane permeability, instability in the gastrointestinal tract, and extensive metabolism in the body. To enhance the bioavailability of ginsenosides, diverse micro-/nano-sized delivery systems such as emulsions, polymeric particles, and vesicular systems have been investigated. The delivery systems improved the bioavailability of ginsenosides by enhancing solubility, permeability, and stability of the natural products. This mini-review aims to provide comprehensive information on the micro-/nano-sized delivery systems for increasing the bioavailability of ginsenosides, which may be helpful for designing better delivery systems to maximize the versatile therapeutic potential of ginsenosides.

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A combined wire structure, made up of longer periodic Si microwires and short nanoneedles, was prepared to enhance light absorption using one-step plasma etching via lithographical patterning. The combined wire array exhibited light absorption of up to ~97.6% from 300 to 1100 nm without an anti-reflection coating. These combined wire arrays on a Si substrate were embedded into a transparent polymer. A large-scale wire-embedded soft film was then obtained by peeling the polymer-embedded wire portion from the substrate. Optically attractive features were present in these soft films, making them suitable for use in flexible silicon solar cell applications.

Background Growth factors (GFs) are signaling proteins that affect cellular processes such as growth, proliferation, and differentiation. GFs are used as cosmeceuticals, exerting anti-wrinkle, anti-aging, and whitening effects, and also as pharmaceuticals to treat wounds, growth failure, and oral mucositis. However, in mammalian and bacterial cells, low productivity and expression in inclusion bodies, respectively, of GFs does not satisfy the consumer demand. Here, we aimed to develop a bacterial expression system that produces high yields of soluble GFs that can be purified in their native forms. Results We present Fh8, an 8-kDa peptide from Fasciola hepatica with an N-terminal hexa-histidine (6HFh8), as a fusion partner for enhanced human GF production in recombinant Escherichia coli. The fusion partner harboring a tobacco etch virus (TEV) protease cleavage site was fused to the N-terminus of 10 human GFs: acidic and basic fibroblast growth factors (aFGF and bFGF, respectively), epidermal growth factor (EGF), human growth hormone (hGH), insulin-like growth factor 1 (IGF-1), vascular endothelial growth factor 165 (VEGF165), keratinocyte growth factor 1 (KGF-1), placental growth factor (PGF), stem cell factor (SCF), and tissue inhibitor of metalloproteinase 1 (TIMP-1). The fusion proteins were expressed in E. coli under the control of T7 promoter at three temperatures (25 °C, 30 °C, and 37 °C). All individual fusion proteins, except for SCF and TIMP-1, were successfully overexpressed in cytoplasmic soluble form at more than one temperature. Further, the original aFGF, IGF-1, EGF, and VEGF165 proteins were cleaved from the fusion partner by TEV protease. Five-liter fed-batch fermentation approaches for the 6HFh8-aFGF (lacking disulfide bonds) and 6HFh8-VEGF165 (a cysteine-rich protein) were devised to obtain the target protein at concentrations of 9.7 g/l and 3.4 g/l, respectively. The two GFs were successfully highly purified (> 99% purity). Furthermore, they exerted similar cell proliferative effects as those of their commercial equivalents. Conclusions We demonstrated that 6HFh8-GF fusion proteins could be overexpressed on a g/l scale in the cytoplasm of E. coli, with the GFs subsequently highly purified and maintaining their biological activity. Hence, the small protein 6HFh8 can be used for efficient mass-production of various GFs.