Highly Stable Au Nanoparticles with Tunable Spacing and Their Potential Application in Surface Plasmon Resonance Biosensors

Colloidal Au‐amplified surface plasmon resonance (SPR), like traditional SPR, is typically used to detect binding events on a thin noble metal film. The two major concerns in developing colloidal Au‐amplified SPR lie in 1) the instability, manifested as a change in morphology following immersion in organic solvents and aqueous solutions, and 2) the uncontrollable interparticle distance, determining probe spacing and inducing steric hindrance between neighboring probe molecules. This may introduce uncertainties into such detecting techniques, degrade the sensitivity, and become the barricade hampering colloidal Au‐based transducers from applications in sensing. In this paper, colloidal Au‐amplified SPR transducers are produced by using ultrathin Au/Al₂O₃ nanocomposite films via a radio frequency magnetron co‐sputtering method. Deposited Au/Al₂O₃ nanocomposite films exhibit superior stability, and average interparticle distances between Au nanoparticles with similar average sizes can be tuned by changing surface coverage. These characteristics are ascribed to the spacer function and rim confinement of dielectric Al₂O₃ and highlight their advantages for application in optimal nanoparticle‐amplified SPR, especially when the probe size is smaller than the target molecule size. This importance is demonstrated here for the binding of protein (streptavidin) targets to the probe (biotin) surface. In this case, the dielectric matrix Al₂O₃ is a main contributor, behaving as a spacer, tuning the concentration of Au nanoparticles, and manipulating the average interparticle distance, and thus guaranteeing an appropriate number of biotin molecules and expected near‐field coupling to obtain optimal sensing performance.     

Improvement of the surface quality of foam injection molded products from a material property perspective

Microcellular injection molding is an attractive method. However, their surface imperfections have been a major problem hindering wide industrial applications. Several methods have been proposed to improve the surface appearance of foams. In this study, we proposed a method to improve the surface appearance of polypropylene (PP) foams from the material property perspective, especially with regard to crystallization and viscosity. The basic idea of the surface improvement is to reduce the size of bubbles generated at the flow front, delay the solidification behavior of the polymer at the mold interface, squeeze the bubbles existing at the mold–polymer interface, and redissolve the bubbles into the polymer by holding pressure. Blending a low-modulus PP delays the crystallization of the polymers at the skin layer and solidification, taking enough time to squeeze the bubbles smaller. A sorbitol-based gelling agent, bis-O-([4 methylphenyl]methylene)-D-Glucitol, was used to increase the viscosity at a low strain rate to reduce the size of the bubbles generated at the flow front during the filling stage. The foam injection molding experiments demonstrated that the proposed method effectively improved the surface appearance of the foams. In particular, the surface appearance of the foams became almost equivalent to that of solid samples using low-modulus PP.     

Functional analysis of genes encoding putative oxidoreductases in Aspergillus oryzae, which are similar to fungal fructosyl-amino acid oxidase

We found 11 genes (FAO1-11) encoding putative oxidoreductases in the Aspergillus oryzae genome, which are similar to fungal fructosyl-amino acid oxidases. The cDNAs corresponding to the genes were cloned and expressed in Escherichia coli. rFao2 had fructosyl-amino acid oxidase activity, whereas rFao1 did not show any enzyme activity, even though the deduced amino acid sequence of Fao1 is identical to that of one of the fructosyl-amino acid oxidase isozymes from Aspergillus oryzae. rFao7 and rFao8 showed oxidase activity toward sarcosine, L-pipecolate, and L-proline. rFao10 was active toward only sarcosine, of the substrates tested. The functions of the other proteins were also predicted from a phylogenetic analysis.     

Application of microalgae hydrolysate as a fermentation medium for microbial production of 2-pyrone 4,6-dicarboxylic acid

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Investigation of localized deformation in partially saturated sand under triaxial compression using microfocus X-ray CT with digital image correlation

In this paper, localized deformation in partially saturated sand was investigated quantitatively using microfocus X-ray computed tomography (CT) and an image analysis of the CT images. Triaxial compression tests on a partially saturated dense Toyoura sand specimen were carried out under a low confining pressure and under drained conditions for both air and water. The development of localized deformation was observed macroscopically using microfocus X-ray CT, and the displacement field over the entire specimen was quantified by an image analysis of the CT images with the digital image correlation (DIC) technique. The progressive development of shear bands is discussed with reference to these images. In addition, the region of localization was observed microscopically by partial CT scanning on a micron scale with high spatial resolution. Changes in the particulate structures are also discussed herein. The DIC image analysis of the partial CT images provided a microscopic displacement field and indicated that very fine localized shear deformation developed before the shear bands had become visible in the macroscopic investigation.     

Development of a Simplified Calculation Tool for Voltage Drop Caused by Transformer Inrush in Distribution System

It is well known that a voltage drop due to inrush current at an energizing transformer may at times interrupt electrical equipment. Generally, the voltage drop is calculated by using a sophisticated tool such as EMTP, so that the transformer saturation phenomenon has been properly represented. However, it is not practical for distribution system engineers to calculate the voltage drop with transformer inrush by using EMTP, because there are many network access requests needing such calculations with many kinds of transformers. Therefore, in this paper, a simplified and easy‐to‐use calculation tool for voltage drops caused by transformer inrush in a distribution system is developed. In order to understand the voltage drop by inrush current during the planning stage, it is formulated by considering the transformer saturation/unsaturation periods in each winding type. The newly developed tool is based on versatile spreadsheet software such as Microsoft Excel ýO.R. It can be used with accuracy similar to that of EMTP. © 2013 Wiley Periodicals, Inc. Electr Eng Jpn, 185(1): 36–47, 2013; Published online in Wiley Online Library ( wileyonlinelibrary.com ). DOI 10.1002/eej.22394     

Differential expression of alpha 1(IV), alpha 2(IV), alpha 5(IV) and alpha 6(IV) collagen chains in the basement membrane of basal cell carcinoma

Type IV collagen, the major component of basement membrane, consists primarily of alpha 1(IV) and alpha 2(IV) chains. Recently, other types of collagen IV chains, i.e. alpha 3(IV), alpha 4(IV), alpha 5(IV) and alpha 6(IV) chains, have been identified by protein chemistry and molecular cloning. We have examined the diversity of the assembly of alpha (IV) chains of the basement membrane surrounding tumour nests of basal cell carcinomas, in tissues from 11 patients, by immunohistochemical analysis using specific monoclonal antibodies to six alpha (IV) chain. The immunostaining profile of each chain differed with respect to the histological subtypes of basal cell carcinoma. In the morphea-like subtype, which was more invasive, alpha 1(IV) and alpha 2(IV) chains were discontinuously stained, and alpha 5(IV) and alpha 6(IV) chains were entirely absent. However, in the superficial subtype, which was non-aggressive, alpha 1(IV), alpha 2(IV), alpha 5(IV) and alpha 6(IV) chains were well stained compared with the other subtypes of basal cell carcinoma. In addition, in the solid subtype, which showed slow growth and ulceration, alpha 1(IV) and alpha 2(IV) chains were continuously stained, and alpha 5(IV) and alpha 6(IV) chains were discontinuous or absent. The assembly of alpha 5(IV) and alpha 6(IV) chains into the basement membrane was inhibited in the solid and morphea subtypes of BCC. This differential expression of type IV collagen chains seems to be associated with the invasive potential of basal cell carcinoma.     

Hydroboration copolymerization

Summary Organoboron copolymers were prepared by polyaddition of diene mixture or diene/diyne mixture, respectively, with thexylborane (1). When a mixture of dienes such as 1,2-diallyloxyethane (2a) and p-diallylbenzene (2b) was polymerized with 1, the peaks in GPC using both UV and RI detectors were shifted to higher molecular weight regions with the increase of the amount of 1. The molecular weight distribution of the copolymer obtained by this method indicated clear difference from that of a mixture of two homopolymers. On the other hand, when the poymerization between 1 and 1,7-octadiene (2c) was carried out in the presence of a trace amount of 1,7-octadiyne (4), the molecular weights of organoboron polymers were found to be increased when the ratio of 4/2c was increased.     

Structure of the human type XIX collagen (COL19A1) gene, which suggests it has arisen from an ancestor gene of the FACIT family

Type XIX collagen is a newly discovered member of the FACIT (fibril-associated collagens with interrupted triple helices) group of extracellular matrix proteins. Based on the primary structure, type XIX collagen is thought to act as a cross-bridge between fibrils and other extracellular matrix molecules. Here we describe the complete exon/intron organization of COL19A1 and show that it contains 51 exons, spanning more than 250 kb of genomic DNA. The comparison of exon structures of COL19A1 and other FACIT family genes revealed several similarities among these genes. The structure of exons encoding the noncollagenous (NC) 1-collagenous (COL) 1-NC 2-COL 2-NC 3-COL 3-NC 4 domain of the alpha1(XIX) chain is similar to that of the NC 1-COL 1-NC 2-COL 3-NC 3 domain of the alpha2(IX) chain except for the NC 3 domain of alpha1(XIX). The exons encoding the COL 5-NC 6 domain of alpha1(XIX) are also similar to those of the COL 3-NC 4 domain of alpha1(IX) chain. Previously, COL19A1 was mapped to human chromosome 6q12-q14, where COL9A1 is also located. Likewise, the present work shows that the mouse Col19a1 gene is located on mouse chromosome 1, region A3, where Col9a1 has also been mapped. Taken together, the data suggest that COL19A1 and COL9A1 (Col19a1 and Col9a1) were duplicated from the same ancestor gene of the FACIT family. Three CA repeat markers with high heterozygosity were found in COL19A1. These markers may be useful for linkage analysis of age-related inheritable diseases involved in eyes and/or brain.