Theoretical study of molecular rectification in porphyrin dimer

Carrying out theoretical calculations using the density functional method for nonequilibrium electron transport, we investigated the electric conductibility of a porphyrin dimer coupled to gold electrodes by thiolate bonds. A porphyrin with four electron-donating amino groups in the dimer is connected to a porphyrin with four electron-withdrawing cyano groups by a dimethylene bridge. The calculations demonstrated that this dimer allows more flow of electrons from the first porphyrin (donor) to the second porphyrin (acceptor) than in the opposite direction. This means that the porphyrin dimer has favorable rectifier characteristics that are accounted for by the mechanism of not Aviram and Ratner [Chem. Phys. Lett. 29 (1974) 277] but of Stokbro, et al. [J. Am. Chem. Soc. 125 (2003) 3674].     

Low-dose N omega-nitro-L-arginine methyl ester treatment improves survival rate and decreases myocardial injury in a murine model of viral myocarditis induced by coxsackievirus B3

Recent reports demonstrated the expression of inducible-type NO synthase in the heart of viral myocarditis. Since NO has multiple biological actions, a substantial amount of NO produced in the diseased heart may act either as a cytotoxic or as a cytoprotective molecule in the process of myocarditis. In the present study, we examined the effect of inhibition of NO synthesis on the mortality and the extent of myocardial injury in a murine model of coxsackievirus B3-induced myocarditis. We fed the infected mice drinking water containing a relatively low concentration (0.37 mmol/L) of N omega-nitro-L-arginine methyl ester (L-NAME) for 14 days after virus inoculation. This dose of L-NAME did not change virus titers in the heart. However, L-NAME-fed mice showed a significant reduction in mortality compared with those fed normal drinking water (nontreated mice). On the contrary, mice given a higher concentration of L-NAME (3.7 mmol/L) exhibited increased mortality. In addition, mice fed a low concentration of L-NAME showed reductions in the severity of heart failure and in the area of myocardial necrosis. Although systemic blood pressure was reduced in nontreated mice, in mice fed a low concentration of L-NAME, it was maintained at a level similar to that in uninfected control mice, L-NAME-treated mice also exhibited a reduction in the degree of inflammatory cell infiltration associated with decreased production of tissue prostaglandin E2 levels in the heart compared with nontreated mice. Therefore, NO is likely to be involved in the pathogenic mechanisms of myocardial injury and resultant cardiac dysfunction in a murine model of coxsackievirus B3-induced viral myocarditis.     

Development of fabrication process for Ag/polydiacetylene (core/shell) hybridized nanocrystals

Core/shell hybridized nanocrystals composed of Ag nanoparticle core and polydiacetylene shell were fabricated successfully by means of “co-reprecipitation/microwave irradiation method”. The hybridized nanocrystals were characterized using transmission electron microscopy (TEM) observation and UV–vis absorption spectroscopy. UV–vis spectral measurements revealed that polydiacetylene shell was the red phase while π-conjugated backbone is distorted. Detailed mechanism of formation of the red phase was discussed.     

Site‐Selective Iron(III) Chloride‐Catalyzed Arylation of 4‐Aryl‐4‐methoxy‐2,5‐cyclohexadienones for the Synthesis of Polyarylated Phenols

The iron(III) chloride‐catalyzed Friedel–Crafts arylation of 4‐aryl‐4‐methoxy‐2,5‐cyclohexadienones, which were easily prepared by the phenyliodine(III) diacetate (PIDA)‐mediated oxidation of 4‐arylphenols in methanol, proceeded site‐selectively to form meta‐terphenyl (2,4‐diarylphenol) derivatives in good yields. The subsequent PIDA‐mediated oxidation and iron(III) chloride‐catalyzed Friedel–Crafts arylation of the resulting products gave the corresponding 2,4,6‐triarylphenol derivatives. The present method provides useful highly substituted polyarylated compounds.

     

Specificity of the SH2 domains of SHP-1 in the interaction with the immunoreceptor tyrosine-based inhibitory motif-bearing receptor gp49B

Inhibitory receptors on hemopoietic cells critically regulate cellular function. Despite their expression on a variety of cell types, these inhibitory receptors signal through a common mechanism involving tyrosine phosphorylation of the immunoreceptor tyrosine-based inhibitory motif (ITIM), which engages Src homology 2 (SH2) domain-containing cytoplasmic tyrosine or inositol phosphatases. In this study, we have investigated the proximal signal-transduction pathway of an ITIM-bearing receptor, gp49B, a member of a newly described family of murine NK and mast cell receptors. We demonstrate that the tyrosine residues within the ITIMs are phosphorylated and serve for the association and activation of the cytoplasmic tyrosine phosphatase SHP-1. Furthermore, we demonstrate a physiologic association between gp49B and SHP-1 by coimmunoprecipitation studies from NK cells. To address the mechanism of binding between gp49B and SHP-1, binding studies involving glutathione S-transferase SHP-1 mutants were performed. Utilizing the tandem SH2 domains of SHP-1, we show that either SH2 domain can interact with phosphorylated gp49B. Full-length SHP-1, with an inactivated amino SH2 domain, also retained gp49B binding. However, binding to gp49B was disrupted by inactivation of the carboxyl SH2 domain of full-length SHP-1, suggesting that in the presence of the phosphatase domain, the carboxyl SH2 domain is required for the recruitment of phosphorylated gp49B. Thus, gp49B signaling involves SHP-1, and this association is dependent on tyrosine phosphorylation of the gp49B ITIMs, and an intact SHP-1 carboxyl SH2 domain.