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방주용,정우성,박형순,정경호,이재준,차은희,이재관,Bang, Joo-Yong,Jeong, Woo-Sung,Park, Hyung-Soon,Chung, Kyung-Ho,Nath, Narayan Chandra Deb,Lee, Jae-Joon,Cha, Eun-Hee,Lee, Jae-Kwan 한국전기화학회 2010 한국전기화학회지 Vol.13 No.3
전도성 고분자로 널리 알려진 폴리아닐린과 액체전해질의 핵심 재료인 이온성 액체와의 복합체를 형성시키고 이들의 물리적, 전기화학적인 특성을 조사되었다. 이미다졸늄 이온성 액체 (1-methyl-3-propylimidazolium iodide, PMI-I)에 비전도성 폴리아닐린 (Emeraldine Base)을 30 wt%이상 첨가하였을 때 준고형화 현상이 나타났고, 이온성 액체의 이미다졸늄 양이온의 방향족 고리와 폴리아닐린의 벤족기와의 ${\pi}-{\pi}$ 자기상호조립에 의한 약한 도핑작용을 통해 섬유상 구조를 나타내었으며, 전도도의 변화율은 80%이상 유지하였다. Polyaniline-ionic liquid composite was prepared and investigated its physical and electrochemical properties. The quasi-solidification was presented in imidazolium-based ionic liquid (1-methly-3-propylimidazolium iodide, PMI-I) containing above 30 wt% of polyaniline (emeraldine base), which exhibited around 80% decrease of conductivity compared to pristine ionic liquid, resulting in fibril structure trough ${\pi}-{\pi}$ self-assembled of imidazolium aromatic ring of ionic liquid on polyaniline framework.
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민경환,방주용,김광표,김완섭,이상화,Selina Rahman Shanta,이정화,홍지혜,임소덕,유영범,Chan-Hyun Na 대한의학회 2014 Journal of Korean medical science Vol.29 No.7
Direct tissue imaging mass spectrometry (IMS) by matrix-assisted laser desorptionionization and time-of-flight (MALDI-TOF) mass spectrometry has become increasinglyimportant in biology and medicine, because this technology can detect the relativeabundance and spatial distribution of interesting proteins in tissues. Five thyroid cancersamples, along with normal tissue, were sliced and transferred onto conductive glass slides. After laser scanning by MALDI-TOF equipped with a smart beam laser, images were createdfor individual masses and proteins were classified at 200-μm spatial resolution. Based onthe spatial distribution, region-specific proteins on a tumor lesion could be identified byprotein extraction from tumor tissue and analysis using liquid chromatography withtandem mass spectrometry (LC-MS/MS). Using all the spectral data at each spot, variousintensities of a specific peak were detected in the tumor and normal regions of the thyroid. Differences in the molecular weights of expressed proteins between tumor and normalregions were analyzed using unsupervised and supervised clustering. To verify the presenceof discovered proteins through IMS, we identified ribosomal protein P2, which is specificfor cancer. We have demonstrated the feasibility of IMS as a useful tool for the analysis oftissue sections, and identified the tumor-specific protein ribosomal protein P2.
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나찬현,홍지혜,김완섭,Selina Rahman Shanta,방주용,박동민,김학균,김광표 한국분자세포생물학회 2015 Molecules and cells Vol.38 No.7
Since the emergence of proteomics methods, many proteins specific for renal cell carcinoma (RCC) have been identified. Despite their usefulness for the specific diagnosis of RCC, such proteins do not provide spatial information on the diseased tissue. Therefore, the identification of cancerspecific proteins that include information on their specific location is needed. Recently, matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS) based imaging mass spectrometry (IMS) has emerged as a new tool for the analysis of spatial distribution as well as identification of either proteins or small molecules in tissues. In this report, surgical tissue sections of papillary RCC were analyzed using MALDI-IMS. Statistical analysis revealed several discriminative cancer-specific m/z-species between normal and diseased tissues. Among these m/z-species, two particular proteins, S100A11 and ferritin light chain, which are specific for papillary RCC cancer regions, were successfully identified using LC-MS/MS following protein extraction from independent RCC samples. The expressions of S100A11 and ferritin light chain were further validated by immunohistochemistry of human tissues and tissue microarrays (TMAs) of RCC. In conclusion, MALDI-IMS followed by LCMS/ MS analysis in human tissue identified that S100A11 and ferritin light chain are differentially expressed proteins in papillary RCC cancer regions.
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