Diffuse color patterning using blended electrochromic polymers for proof‐of‐concept adaptive camouflage plaques

A study using three different pairs of electrochromic polymers (ECPs) synthesized onto plaques by means of a modified vapor phase polymerization (VPP) technique is presented. Restriction of the respective polymerization times, allowed both faster and slower polymerizing monomers to be controlled, and produced blended plaques with visually diffuse interfaces. The ECPs within the blended plaques retain their individual electrochromic behavior and when encapsulated into an electrochromic device, show outstanding optical switching performance with little degradation evident over 10,000 cycles, coupled with a switching time of the order of 1 second. Blends also allow multiple diffuse color changes within an electrochromic device, due to the difference in oxidation potentials of the individual ECPs, making them candidates for adaptive camouflage use. © 2015 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2015 , 132, 42158.     

Design of Trehalose-Based Amide/Sulfonamide C-type Lectin Receptor Signaling Compounds

Mincle agonists have been shown to induce inflammatory cytokine production, such as tumor necrosis factor-alpha (TNF) and promote the development of a Th1/Th17 immune response that might be crucial to development of effective vaccination against pathogens such as Mycobacterium tuberculosis. As an expansion of our previous work, a library of 6,6′-amide and sulfonamide α,α-d -trehalose compounds with various substituents on the aromatic ring was synthesized efficiently in good to excellent yields. These compounds were evaluated for their ability to activate the human C-type lectin receptor Mincle by the induction of cytokines from human peripheral blood mononuclear cells. A preliminary structure–activity relationship (SAR) of these novel trehalose diamides and sulfonamides revealed that aryl amide-linked trehalose compounds demonstrated improved activity and relatively high potency cytokine production compared to the Mincle ligand trehalose dibehenate adjuvant (TDB) and the natural ligand trehalose dimycolate (TDM) inducing dose-dependent and human-Mincle-specific stimulation in a HEK reporter cell line.     

Formulation of a ceramic ink for a wide-array drop-on-demand ink-jet printer

This paper describes the methodology for simulating a reprographic ink with a ceramic ink based on a commercially available zirconia powder for direct ceramic ink-jet printing. Of over-riding importance was matching viscosity and this was tested systematically by using a mineral oil–hexane binary system. Of secondary importance was adjustment of the pressure defect behind the nozzle to compensate for small differences in surface tension. The inks tested in the wide array print-head were based on low electrical conductivity liquids to avoid damage to the electroding system. The organic binder for the zirconia ink was paraffin wax and the dispersant was a hydroxystearic acid based polyester.     

A noncompetitive peptide inhibitor of the nicotinic acetylcholine receptor from Conus purpurascens venom

A paralytic peptide, psi-conotoxin Piiie has been purified and characterized from Conus purpurascens venom. Electrophysiological studies indicate that the peptide inhibits the nicotinic acetylcholine receptor (nAChR). However, the peptide does not block the binding of alpha-bungarotoxin, a competitive nAChR antagonist. Thus, psi-conotoxin Piiie appears to inhibit the receptor at a site other than the acetylcholine-binding site. As ascertained by sequence analysis, mass spectrometry, and chemical synthesis, the peptide has the following covalent structure: HOOCCLYGKCRRYOGCSSASCCQR* (O = 4-trans hydroxyproline; * indicates an amidated C-terminus). The disulfide connectivity of the toxin is unrelated to the alpha- or the alphaA-conotoxins, the Conus peptide families that are competitive inhibitors of the nAChR, but shows homology to the mu-conotoxins (which are Na+ channel blockers).     

A magnetic resonance imaging study of planum temporale asymmetry in men with developmental dyslexia

The influence of ionic strength and composition on the binding and inhibition of human leukocyte elastase by glycosaminoglycans with variable degree and position of sulfation was investigated. The kinetic mechanism of inhibition had a hyperbolic, mixed-type character with a competitive component that was promoted by low ionic strength, reduced by phosphate ions, and which also depended on the substrate and glycosaminoglycan structure. Enzyme binding was a cooperative phenomenon that varied with ionic strength and composition. The inhibition patterns correlated with the cationic character of elastase and with the distribution of arginines on its molecular surface, most notably with residues located in the vicinity of the substrate binding region. The order of affinity for elastase binding was chondroitin 4-sulfate < chondroitin 6-sulfate < dermatan sulfate, iduronate-containing derivatives being superior with respect to the glucuronate-containing counterparts. Additional sulfation at both the 4- and 6- positions or at the N- and 4-positions of the N-acetylgalactosamine moiety decidedly improved the inhibitory efficiency. The results highlight a fundamental physiological role of enzyme-glycosaminoglycan interactions. In the azurophil granule of the human polymorphonuclear neutrophil, elastase and other enzymes are bound to a matrix of chondroitin 4-sulfate because this is the only glycosaminoglycan that simultaneously offers good binding for enzyme compartmentalization together with prompt release from the bound state at the onset of phagocytosis.