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Kim, A.,Park, E.,Lee, H.,Kim, H. ELSEVIER SCIENCE 2016 Journal of Alloys and Compounds Vol.681 No.-
MoO<SUB>2</SUB> has gained renewed attention as a safe oxide anode host material for lithium ion insertion because of its high gravimetric/volumetric capacity and highly stable cycling behavior. However, these recent results are completely contrary to previous reports. To confirm that MoO<SUB>2</SUB> is an appropriate anode material as well as further understand lithium ion reactions when inserted into MoO<SUB>2</SUB>, we combine electrochemical characterization of MoO<SUB>2</SUB> electrodes and ex situ X-ray diffraction analysis with first principle calculations. Theoretical capacity of the MoO<SUB>2</SUB> electrode (~209 mAh g<SUP>-1</SUP>) and stable capacity retention up to 100 cycles are simultaneously attained using a proper particle size and type of binder. Ex situ XRD analysis with first principle calculations of the phase transformation of MoO<SUB>2</SUB> electrodes shows that MoO<SUB>2</SUB> undergoes reversible structural changes upon lithiation and subsequent delithiation, clearly demonstrating that nanostructured MoO<SUB>2</SUB> can be used as an anode material for highly reliable lithium ion batteries.
Synthesis and antibacterial evaluation of hamacanthin B analogues
Kim, A.,Kim, M.J.,Noh, T.H.,Hong, J.,Liu, Y.,Wei, X.,Jung, J.H. Pergamon Press 2016 Bioorganic & medicinal chemistry letters Vol.26 No.20
Hamacanthins are a class of antibacterial bisindole alkaloids isolated from marine sponges. Based on structure-activity relationships and in silico MRSA PK binding analysis of these bisindole alkaloids, the authors designed new hamacanthin B derivatives and evaluated their antibacterial activities against drug-resistant pathogens. Racemates of the synthetic products were resolved into their enantiomers by chiral separation using a cellulose column, and antibacterial activities were compared. Unsaturation of the central heterocyclic ring structure and bromine substitution at the indole moiety were found to enhance the antibacterial activities of hamacanthin B analogues.
Kim, A.,Lee, J.,Kim, B.G.,Lee, D.J.,Jung, H. Elsevier [etc.] 2017 Journal of luminescence Vol.190 No.-
The fluorescent solid material, which emits highly efficient deep-blue light, was successfully fabricated by stabilized 9,10-diphenylanthracene (DPA) molecules in mesostructured silica material (MSM) (referred to as DPA-MSM). The DPA molecules are favorably introduced into the hydrophobic domain of a self-assembled amphiphilic triblock copolymer (poly(ethylene glycol)-block-poly(propylene glycol)-block-poly(ethylene glycol), Pluronic P123) template through a one-pot synthetic route based on the van der Waals interaction. Powder X-ray diffraction patterns show that the unit-cell parameter of DPA-MSM was 1.2nm larger than that of pure MSM, along with the well-ordered hexagonal structure. The photophysical properties of DPA-MSM have been studied and compared with those of DPA in solution (0.15mM) and powdered states, respectively. Both absorption and emission maxima of the immobilized DPA show a remarkable hypsochromic shift as compared with those of pure DPA powder. In addition, we have observed distinct spectral features in the DPA-MSM, which resemble those of DPA dissolved in cyclohexane, indicating that the immobilized DPA is molecularly separated by the interactions with the poly(propylene glycol) part in P123. The fluorescence decay behavior showed that DPA-MSM has a longer lifetime because the intramolecular motions of DPA are strongly restricted by the confined environment within the pore channel of rigid MSM. These results also show that the immobilized DPA has a higher fluorescence quantum yield than did DPA in dissolved or powdered states. The fabricated blue LED chip with DPA-MSM exhibited outstanding deep-blue color with CIE coordinates of (0.15, 0.03). It was found that the incorporation of DPA in MSM provides an efficient blue emitter in the solid-state.
Kim, A.,Im, M.,Ma, J. Y. Spandidos Publications 2016 Oncology reports Vol.35 No.3
<P>Cachexia accompanied by muscle wasting is a key determinant of poor prognosis in cancer patients and cancer-related death. Previous studies have demonstrated that inflammatory cytokines such as interleukin-6 (IL-6), tumor necrosis factor-alpha (TNF-alpha), IL-1 and interferon-gamma (IFN-gamma) secreted from host cells and tumor cells participate in skeletal muscle wasting followed by severe loss of body weight. Therefore, blockade of the inflammatory response is thought to be a logical target for pharmacological and nutritional interventions to preserve skeletal muscle mass under cachectic conditions. Sosiho-tang (SO; Xiaocharihu-tang in Chinese and Sho-saiko-to in Japanese) is an Oriental herbal medicine that has been used to treat chronic hepatic diseases and to control fever. In recent studies, SO inhibited the production of inflammatory cytokines in lipopolysaccharide (LPS)-stimulated macrophages, prevented thrombus formation and suppressed cancer progression. However, the anti-cachectic activity of SO in tumor-bearing mice has not yet been examined. In the present study, we characterized the effect of SO administration on cancer-induced cachexia in CT-26-bearing mice, and elucidated the anti-cachectic mechanisms. Daily oral administration of SO at doses of 50 and 100 mg/kg to CT-26-bearing mice significantly retarded tumor growth and prevented the loss of final body weight, carcass weight, heart weight, gastrocnemius muscle, and epididymal fat, compared with saline-treated control mice. In addition, serum IL-6 levels elevated by cancer were decreased by SO administration. In the J774A.1 macrophage cell line, SO efficiently suppressed LPS-mediated increases in inducible nitric oxide synthase (iNOS) expression, nitric oxide (NO), and procachectic inflammatory cytokine production through inhibition of nuclear factor-kappa B (NF-kappa B) and p38 activation. In addition, SO attenuated muscle atrophy caused by cancer cells by affecting myoblast proliferation and differentiation, and C2C12 myotube wasting. Taken together, these results suggest that SO is a safe and useful anti-cachectic therapy for cancer patients with severe weight loss.</P>
Kim, A.,Lee, J.Y.,Byun, S.J.,Kwon, M.H.,Kim, Y.S. Elsevier/North-Holland 2012 Antiviral research Vol.94 No.2
Influenza A virus infection is a great threat to avian species and humans. Targeting viral proteins by antibody has a limited success due to the antigen drift and shift. Here we present a novel antibody-based antiviral strategy of targeting viral genomic RNA (vRNA) for degradation rather than neutralizing viral proteins. Based on the template of a sequence-nonspecific nucleic acid-hydrolyzing, single domain antibody of the light chain variable domain, 3D8 VL, we generated a synthetic library on the yeast surface by randomizing putative nucleic acid interacting residues. To target nucleocapsid protein (NP)-encoding viral genomic RNA (NP-vRNA) of H9N2 influenza virus, the library was screened against a 18-nucleotide single stranded nucleic acid substrate, dubbed asNP<SUB>18</SUB>, the sequence of which is unique to the NP-vRNA. We isolated a 3D8 VL variant, NP25, that had ~15-fold higher affinity (~54nM) and ~3-fold greater selective hydrolyzing activity for the target substrate than for off targets. In contrast to 3D8 VL WT, asNP<SUB>18</SUB>-selective NP25 constitutively expressed in the cytosol of human lung carcinoma A549 cells does not exhibit any significant cytotoxicity and selectively degrades a reporter mRNA carrying the target asNP<SUB>18</SUB> sequence in the stable cell lines. NP25 more potently inhibits the replication of H9N2 influenza virus than 3D8 VL WT in the stable cell lines. NP25 more selectively reduces the amount of the targeted NP-vRNA than 3D8 VL WT from the early stage of virus infection in the stable cell lines, without noticeable harmful effects on the endogenous mRNA, suggesting that NP25 indeed more specifically recognizes to hydrolyze the target NP-vRNA of H9N2 virus than off-targets. Our results provide a new strategy of targeting viral genomic RNA for degradation by antibody for the prevention of influenza virus infection in humans and animals.