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Bovine diarrhea is a major concern in the global bovine industry because it can cause significant financial damage. Of the many potential infectious agents that can lead to bovine diarrhea, bovine rotavirus (BRV) is a particular problem due to its high transmissibility and infectivity. Therefore, it is important to prevent the proliferation of BRV using an early detection system. This study developed an affinity peptide-based electrochemical method for use as a rapid detection system for BRV. A BRV-specific peptide was identified via the phage display technique and chemically synthesized. The synthetic peptide was immobilized on a gold electrode through thiol-gold interactions. The performance of the BRV specific binding peptides was evaluated using square wave voltammetry. The developed detection system exhibited a low detection limit (5 copies/mL) and limit of quantitation (2.14 × 10

Muscle tissue influences energy and protein metabolism throughout the body. Earlier reports demonstrated that bone morphogenetic protein 11 (BMP11) could inhibit skeleton muscle proliferation and development. However, the role of BMP11 in the fatty acid metabolism of muscle has not been explored. In this study, we investigated the physiological functions of exogenous BMP11 on lipid metabolism in C2C12 cells using recombinant BMP11 (rBMP11). Treatment by rBMP11 inhibits myogenesis while inducing lipid accumulation in C2C12 cells. Moreover, induction of rBMP11 inhibits not only fatty acid uptake by downregulation of the fatty acid transport proteins CD36, FATP1, FATP4, and FABP3 but also suppresses fatty acid oxidation by decreasing the levels of p-HSL, ATGL, ACSL, and CGI-58 via Smad 2/3 pathway. Taken together, BMP11 negatively regulates lipid metabolism in muscle cells, which is an opposite result to that in adipocytes where BMP11 improves metabolic homeostasis. Considering the contrasting roles of BMP11 in adipocytes and muscle cells, BMP11 could be a promising target for pharmacological intervention in the treatment of metabolic diseases.

In this study, we developed an affinity peptide-guided plasmonic biosensor that is capable of detection for noroviral capsid proteins and human norovirus. Construction of plasmonic biosensor was achieved by immobilization of affinity peptides (named norovirus binding peptides) on the localized surface plasmonic sensor (LSPR) layer for detection of noroviral capsid proteins and human norovirus. The performance of the plasmonic biosensor in detection of their targets was monitored using LSPR techniques. This specific interaction is proportional to the absorbance of LSPR signals. The lowest detection value for noroviral capsid protein was 0.1 ng/mL in the presence of complex tissue culture media (MEM and FBS), and limit of detection (LOD) for human norovirus was found to be 9.9 copies/mL by the 3-σ rule. Interestingly, no dynamic binding response with norovirus binding peptides as affinity reagent was observed against rotavirus, suggesting that norovirus binding peptides have high selectivity for human norovirus. Thus, norovirus binding peptide-guided plasmonic biosensor could be used for the detection of norovirus-related foodborne pathogens.

Natural pigments have several advantages over synthetic colorants. In this study, the production of red pigment produced by Paecilomyces sinclairii in microbial fermentation was demonstrated and the pigment was purified and characterized. The red pigment was produced from submerged fungal fermentation and fractionated by medium pressure flash chromatography. After fractionation, the spectrophotometric characterization of the red pigment revealed an λmax at 520 nm. Antimicrobial activity of the red pigment fraction was also studied against Escherichia coli O157 and Pseudomonas aeruginosa PAO1. The fraction (F2-F6) of the red pigment exhibited broad-spectrum antimicrobial activity in both bacteria. These results demonstrate the potential of this pigment in inhibiting bacterial growth and in food processing and other foodrelated applications.

Hizikia fusiforme is a commonly used food that possesses potent anti-bacterial, anti-fungal, and anti-inflammatory activities. The immunostimulatory activities of aqueous extract of Hizikia fusiforme (HFAE) in RAW 264.7 macrophages and whole spleen cells were investigated. HFAE activated RAW 264.7 macrophages to produce cytokines such as nitric oxide (NO), tumor necrosis factor-α (TNF-α), interleukin-1β (IL-1β), and interleukin-6 (IL-6) in a dose-dependent manner. In addition, HFAE induced the mRNA expression of TNF-α, IL-1β, and IL-6 in RAW 264.7 macrophages. Moreover, HFAE stimulated proliferation of whole spleen cells and reference mitogen. Taken together, the results demonstrate that HFAE potently activates the immune function by regulating NO, TNF-α, IL-1β, and IL-6 in RAW 264.7 macrophage and promoting spleen cell proliferation.

Many classes of bioactive drug-like molecules derived from traditional herbal plants are becoming attractive as alternative medicines for the treatment of severe chronic diseases such as cancer and obesity. A set of chemically synthesized drugs that is capable of both inhibiting cancer growth and reducing body weight for treatment of obesity have severe side effects including nausea, vomiting, diarrhea as well as producing increased blood pressure and headache, respectively. For decades, drug candidates from herbal plants have been considered as potential therapeutic agents because they are generally safer, less toxic, and have fewer lethal side effects than chemically synthesized or semi-synthetic drugs. Understanding the key factors affecting pharmacological effects and clinical outcomes has been a critical theme of natural product research. However, standardized sample preparation methods, well-controlled scientific studies, and validation studies are needed before herbal therapeutics can be introduced into the global market. This review will address the current advances in using traditional herbal plants, including the pharmacological effects and the challenges faced during the development of new drugs. The safety issues associated with toxicity and the effectiveness of the herbs in specific diseases such as cancer and obesity are also discussed.

Carbohydrate-protein interaction is one of the most important molecular events deemed critical for numerous biological processes. Therefore, understanding this interaction is essential. In this study, we used bacterial spore display techniques to present multiple copies of streptavidin on the surface of spores to explore carbohydrate-protein interaction in solution and on chips. By applying bacterial spores displaying streptavidin, we developed a new method which allows sensitive, versatile, and passive detection of carbohydrate-protein interactions with a 10-fold increase in sensitivity. The linear relationship of interactions between carbohydrates and labeled concanavalin A (con A) in solution and on functionalized bacterial spore chips has also been confirmed. To the best of our knowledge, this is the first example of development and characterization of binding behavior in carbohydrateprotein interactions using bacterial spore-displayed streptavidin. We believe this strategy may enable new high-throughput screening of carbohydrate interactions as well as establish a basis for monitoring inhibitors of carbohydrate-binding proteins when developing new drugs.

In this study, a simple procedure is described for patterning biotin on a glass substrate and then selectively immobilizing proteins of interest onto the biotin-patterned surface. Microcontact printing (μCP) was used to generate the micropattern of biotin and to demonstrate the selective immobilization of proteins by using enhanced green fluorescent protein (EGFP) as a model protein, of which the C-terminus was fused to a core streptavidin (cSA) gene ofStreptomyces avidinii. Confocal fluorescence microscopy was used to visualize the pattern of the immobilized protein (EGFP-cSA), and surface plasmon resonance was used to characterize biological activity of the immobilized EGFP-cSA. The results suggest that this strategy, which consists of a combination of μμCP and cSA-fused proteins, is an effective way for fabricating biologically active substrates that are suitable for a wide variety of applications, one such being the use in protein-protein assays.

In this study, a novel strategy was developed for the highly selective immobilization of proteins, using the polyhydroxyalkanoate (PHA) depolymerase substrate binding domain (SBD) as an active binding domain. In order to determine the appropriacy of this method for immunodiagnostic assays, the single-chain antibody (ScFv) against the hepatitis B virus (HBV) preS2 surface protein and the severe acute respiratory syndrome coronavirus (SARS-CoV) envelope protein (SCVe) were fused to the SBD, then directly immobilized on PHA-coated slides via microspotting. The fluorescence-labeled HBV antigen and the antibody against SCVe were then utilized to examine specific interactions on the PHA-coated surfaces. Fluorescence signals were detected only at the spotted positions, thereby indicating a high degree of affinity and selectivity for their corresponding antigens/antibodies. Furthermore, we detected small amounts of ScFv-SBD (2.7 ng/mL) and SCVe-SBD fusion proteins (0.6 ng/mL). Therefore, this microarray platform technology, using PHA and SBD, appears generally appropriate for immunodiagnosis, with no special requirements with regard to synthetic or chemical modification of the biomolecules or the solid surface.