A uniform amorphous carbon coating on the tin nanoparticles was prepared from aqueous glucose solutions using a hydrothermal method at 180 °C, which facilitated an enhanced dimensional stability during Li alloying/dealloying. This material showed excellent initial capacity and capacity retention, 681 mAh/g and 98% retention after 50 cycles, respectively.

This study aimed to evaluate particle emission characteristics and to evaluate several control methods used to reduce particle emissions during three-dimensional (3D) printing. Experiments for particle characterization were conducted to measure particle number concentrations, emission rates, morphology, and chemical compositions under manufacturer-recommended and consistent-temperature conditions with seven different thermoplastic materials in an exposure chamber. Eight different combinations of the different control methods were tested, including an enclosure, an extruder suction fan, an enclosure ventilation fan, and several types of filter media. We classified the thermoplastic materials as high emitter (>10 #/min), medium emitters (10 #/min -10 #/min), and low emitters (<10 #/min) based on nanoparticle emissions. The nanoparticle emission rate was at least 1 order of magnitude higher for all seven filaments at the higher consistent extruder temperature than at the lower manufacturer-recommended temperature. Among the eight control methods tested, the enclosure with a high-efficiency particulate air (HEPA) filter had the highest removal effectiveness (99.95%) of nanoparticles. Our recommendations for reducing particle emissions include applying a low temperature, using low-emitting materials, and instituting control measures like using an enclosure around the printer in conjunction with an appropriate filter (e.g., HEPA filter) during 3D printing.

In Saccharomyces cerevisiae, transport of arginine into the vacuole has previously been shown to be facilitated by a putative H ؉ ͞ arginine antiport. We confirm that transport of arginine into isolated yeast vacuoles requires ATP and we demonstrate a requirement for a functional vacuolar H ؉ -ATPase. We previously reported that deletion of BTN1 (btn1-⌬), an ortholog of the human Batten disease gene CLN3, resulted in a decrease in vacuolar pH during early growth. We report that this altered vacuolar pH in btn1-⌬ strains underlies a lack of arginine transport into the vacuole, which results in a depletion of endogenous vacuolar arginine levels. This arginine transport defect in btn1-⌬ is complemented by expression of either BTN1 or the human CLN3 gene and strongly suggests a function for transport of, or regulation of the transport of, basic amino acids into the vacuole or lysosome for yeast Btn1p, and human CLN3 protein, respectively. We propose that defective transport at the lysosomal membrane caused by an absence of functional CLN3 is the primary biochemical defect that results in Batten disease.

Dramatic morphological changes are observed in the Langmuir-Blodgett (LB) film assemblies of poly(ethylene glycol)-b-(styrene-r-benzocyclobutene) block copolymer (PEG-b-(S-r-BCB)) after intramolecular cross-linking of the S-r-BCB block to form a linear-nanoparticle structure. To isolate architectural effects and allow direct comparison, the linear block copolymer precursor and the linear-nanoparticle block copolymer resulting from selective intramolecular cross-linking of the BCB units were designed to have exactly the same molecular weight and chemical composition but different architecture. It was found that the effect of architecture is pronounced with these macromolecular isomers, which self-assemble into dramatically different surface aggregates. The linear block copolymer forms disklike surface assemblies over the range of compression states, while the linear-nanoparticle block copolymer exhibits long (>10 microm) wormlike aggregates whose length increases as a function of increasing cross-linking density. It is shown that the driving force behind the morphological change is a combination of the altered molecular geometry and the restricted degree of stretching of the nanoparticle block because of the intramolecular cross-linking. A modified approach to interpret the pi-A isotherm, which includes presence of the block copolymer aggregates, is also presented, while the surface rheological properties of the block copolymers at the air-water interface provide in-situ evidence of the aggregates' presence at the air-water interface.

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A novel Co-glutarate, Co[O(2)C(CH(2))(3)CO(2)] (1), was synthesized as single crystals by the hydrothermal reaction of CoCl(2) with glutaric acid in the presence of KOH and characterized by single-crystal X-ray diffraction analysis, TGA, IR, UV-vis reflectance spectrometry, and SQUID measurements. The dark purple Co-glutarate crystallizes in the monoclinic system in the space group P2/c, with a = 14.002(3) A, b = 4.8064(10) A, c = 9.274(3) A, beta = 90.5(2)degrees, and Z = 4. The Co(2+) centers are tetrahedrally coordinated to four oxygen atoms from the dicarboxylate ligands. The anhydrous-pillared three-dimensional structure consists of infinite Co-CO(2)-Co inorganic layers, which are stacked by the coordinated glutarate alkyl chain along the a-axis. There are two different conformations for glutarate ligands, i.e., the gauche- and the anti-forms. These ligands reside between the inorganic layers alternatively to separate each layer by 7.01 A (gauche) and 6.99 A (anti). Magnetic measurement reveals that the predominant magnetic interactions are antiferromagnetic below 14 K.

Btn2p, a novel cytosolic coiled-coil protein in Saccharomyces cerevisiae, was previously shown to interact with and to be necessary for the correct localization of Rhb1p, a regulator of arginine uptake, and Yif1p, a Golgi protein. We now report the biochemical and physical interactions of Btn2p with Ist2p, a plasma membrane protein that is thought to have a function in salt tolerance. A deletion in Btn2p (btn2⌬ strains) results in a failure to correctly localize Ist2p, and strains lacking Btn2p and Ist2p (btn2⌬ ist2⌬ strains) are unable to grow in the presence of 0.5 or 1.0 M NaCl. Btn2p was originally identified as being up-regulated in a btn1⌬ strain, which lacks the vacuolar-lysosomal membrane protein, Btn1p, and serves as a model for Batten disease. This up-regulation of Btn2p was shown to contribute to the maintenance of a stable vacuolar pH in the btn1⌬ strain. Btn1p was subsequently shown to be required for the optimal transport of arginine into the vacuole. Interestingly, btn1⌬ ist2⌬ strains are also unable to grow in the presence of 0.5 or 1.0 M NaCl, and ist2⌬ suppresses the vacuolar arginine transport defect in btn1⌬ strains. Although further investigation is required, we speculate that altered vacuolar arginine transport in btn1⌬ strains represents a mechanism for maintaining or balancing cellular ion homeostasis. Btn2p interacts with at least three proteins that are seemingly involved in different biological functions in different subcellular locations. Due to these multiple interactions, we conclude that Btn2p may play a regulatory role across the cell in response to alterations in the intracellular environment that may be caused by changes in amino acid levels or pH, a disruption in protein trafficking, or imbalances in ion homeostasis resulting from either genetic or environmental manipulation.