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Choi, Insoo,Kim, Hak-Yoon,Ahn, Sang Hyun,Hwang, Seung Jun,Yoo, Sung Jong,Kim, Ho Young,Choi, Jihui,Park, Hyan Joo,Jang, Jong Hyun,Kim, Soo-Kil American Scientific Publishers 2016 Journal of nanoscience and nanotechnology Vol.16 No.10
<P>Electrochemical conversion of carbon dioxide to formic acid was attempted on Sn-Zn alloy catalysts. The alloy catalysts were fabricated by electrodeposition, and their compositions were controlled by varying the concentration of the precursor solution. A home made proton exchange membrane-based electrochemical cell was used for the reduction of carbon dioxide. The concentration of formic acid produced and the conversion efficiency were determined via electrolysis and high performance liquid chromatography analysis. The effect of the alloy composition on the amount of formic acid generated and the conversion efficiency was evaluated, and alloy composition was found to have a strong influence on these variables. It was thus concluded that the conversion of carbon dioxide to formic acid can be enhanced by alloying Zn with Sn.</P>
Human Serum Albumin-TRAIL Conjugate for the Treatment of Rheumatoid Arthritis
Byeon, Hyeong Jun,Min, Sun Young,Kim, Insoo,Lee, Eun Seong,Oh, Kyung Taek,Shin, Beom Soo,Lee, Kang Choon,Youn, Yu Seok American Chemical Society 2014 Bioconjugate chemistry Vol.25 No.12
<P>Albumin conjugation is viewed as an effective means of protracting short in vivo lifespans of proteins and targeting rheumatoid arthritis (RA). In this study, we present a human serum albumin (HSA) conjugate linked with tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) via a bifunctional PEG derivative (HSA-TRAIL). Prepared HSA-TRAIL was found to have a larger molecular size (∼240 kDa, 15.4 nm) than TRAIL (∼66 kDa, 6.2 nm), and its bioactivity (apoptosis, cytotoxicity, and antiproliferation) was well preserved in Mia Paca-2 cells and mouse splenocytes. The enhanced therapeutic efficacy of HSA-TRAIL was demonstrated in collagen-induced arthritis (CIA) mice. The incidence and clinical scores, expressed as degree of erythema and swelling in HSA-TRAIL-treated mice, were remarkably lower than those of TRAIL-treated mice. The serum levels of pro-inflammatory cytokines IFN-γ, TNF-α, IL-1β, and IL-2 in HSA-TRAIL-treated mice were significantly lower than those of TRAIL-treated mice. Furthermore, HSA-TRAIL accumulated in the hind paws of CIA mice, not in naïve TRAIL mice. Pharmacokinetic profiles of HSA-TRAIL were greatly improved in comparison to those of TRAIL (AUC<SUB>inf</SUB>: 844.1 ± 130.0 vs 36.0 ± 1.2 ng·h/mL; <I>t</I><SUB>1/2</SUB>: 6.20 ± 0.72 vs 0.23 ± 0.01 h, respectively). The HSA-TRAIL conjugate, which presents clear advantages of targeting RA and long systemic circulation by HSA and unique anti-inflammatory efficacy by TRAIL, has potential as a novel treatment for rheumatoid arthritis.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bcches/2014/bcches.2014.25.issue-12/bc500427g/production/images/medium/bc-2014-00427g_0011.gif'></P>
PEGylated apoptotic protein-loaded PLGA microspheres for cancer therapy
Byeon, Hyeong Jun,Kim, Insoo,Choi, Ji Su,Lee, Eun Seong,Shin, Beom Soo,Youn, Yu Seok Dove Medical Press 2015 INTERNATIONAL JOURNAL OF NANOMEDICINE Vol.10 No.-
<P>The aim of the current study was to investigate the antitumor potential of poly (D,L-lactic-<I>co</I>-glycolic acid) microspheres (PLGA MSs) containing polyethylene glycol (PEG)-conjugated (PEGylated) tumor necrosis factor–related apoptosis-inducing ligand (PEG-TRAIL). PEG-TRAIL PLGA MSs were prepared by using a water-in-oil-in-water double-emulsion method, and the apoptotic activities of supernatants released from the PLGA MSs at days 1, 3, and 7 were examined. The antitumor effect caused by PEG-TRAIL PLGA MSs was evaluated in pancreatic Mia Paca-2 cell-xenografted mice. PEG-TRAIL PLGA MS was found to be spherical and 14.4±1.06 μm in size, and its encapsulation efficiency was significantly greater than that of TRAIL MS (85.7%±4.1% vs 43.3%±10.9%, respectively). The PLGA MS gradually released PEG-TRAIL for 14 days, and the released PEG-TRAIL was shown to have clear apoptotic activity in Mia Paca-2 cells, whereas TRAIL released after 1 day had a negligible activity. Finally, PEG-TRAIL PLGA MS displayed remarkably greater antitumor efficacy than blank or TRAIL PLGA MS in Mia Paca-2 cell-xenografted mice in terms of tumor volume and weight, apparently due to increased stability and well-retained apoptotic activity of PEG-TRAIL in PLGA MS. We believe that this PLGA MS system, combined with PEG-TRAIL, should be considered a promising candidate for treating pancreatic cancer.</P>
Hepatitis E Virus Methyltransferase Inhibits Type I Interferon Induction by Targeting RIG-I
( Sangmin Kang ),( Changsun Choi ),( Insoo Choi ),( Kwi-nam Han ),( Seong Woon Roh ),( Jongsun Choi ),( Joseph Kwon ),( Mi-kyung Park ),( Seong-jun Kim ),( Jinjong Myoung ) 한국미생물생명공학회(구 한국산업미생물학회) 2018 Journal of microbiology and biotechnology Vol.28 No.9
The type I interferons (IFNs) play a vital role in activation of innate immunity in response to viral infection. Accordingly, viruses have evolved to employ various survival strategies to evade innate immune responses induced by type I IFNs. For example, hepatitis E virus (HEV) encoded papain-like cysteine protease (PCP) has been shown to inhibit IFN activation signaling by suppressing K63-linked de-ubiquitination of retinoic acid-inducible gene I (RIG-I) and TANK-binding kinase 1 (TBK1), thus effectively inhibiting down-stream activation of IFN signaling. In the present study, we demonstrated that HEV inhibits polyinosinic-polycytidylic acid (poly(I:C))-induced IFN-β transcriptional induction. Moreover, by using reporter assay with individual HEV-encoded gene, we showed that HEV methyltransferase (MeT), a nonstructural protein, significantly decreases RIG-I-induced IFN-β induction and NF-κB signaling activities in a dose-dependent manner. Taken together, we report here that MeT, along with PCP, is responsible for the inhibition of RIG-I-induced activation of type I IFNs, expanding the list of HEV-encoded antagonists of the host innate immunity.