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RISS 인기검색어
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- 저자 : Heeyoun Chi (검색결과 3 건)
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Lee, Ju Yeon,Lee, Hyun Kyoung,Park, Gun Wook,Hwang, Heeyoun,Jeong, Hoi Keun,Yun, Ki Na,Ji, Eun Sun,Kim, Kwang Hoe,Kim, Jun Seok,Kim, Jong Won,Yun, Sung Ho,Choi, Chi-Won,Kim, Seung Il,Lim, Jong-Sun,Jeo American Chemical Society 2016 JOURNAL OF PROTEOME RESEARCH Vol.15 No.12
<P>Glycoprotein conformations are complex and heterogeneous. Currently, site-specific characterization of glycopeptides is a challenge. We sought to establish an efficient method of N-glycoprotein characterization using mass spectrometry (MS). Using alpha-1-acid glycoprotein (AGP) as a model N-glycoprotein, we identified its tryptic N-glycopeptides and examined the data reproducibility in seven laboratories running different LC-MS/MS platforms. We used three test samples and one blind sample to evaluate instrument performance with entire sample preparation workflow. 165 site-specific N-glycopeptides representative of all N-glycosylation sites were identified from AGP 1 and AGP 2 isoforms. The glycopeptide fragmentations by collision-induced dissociation or higher-energy collisional dissociation (HCD) varied based on the MS analyzer. Orbitrap Elite identified the greatest number of AGP N-glycopeptides, followed by Triple TOF and Q-Exactive Plus. Reproducible generation of oxonium ions, glycan-cleaved glycopeptide fragment ions, and peptide backbone fragment ions was essential for successful identification. Laboratory proficiency affected the number of identified N-glycopeptides. The relative quantities of the 10 major N-glycopeptide isoforms of AGP detected in four laboratories were compared to assess reproducibility. Quantitative analysis showed that the coefficient of variation was <25% for all test samples. Our analytical protocol yielded identification and quantification of site-specific N-glycopeptide isoforms of AGP from control and disease plasma sample.</P>
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Ju Yeon Lee,Hyun Kyoung Lee,Gun Wook Park,Heeyoun Hwang,Hoi Keun Jeong,Ki Na Yun,Eun SunJ i,Kwang Hoe Kim,Jun Seok Kim,Jong Won Kim,Sung Ho Yun,Chi-Won Choi,Seung Il Kim,Jong-Sun Lim,Seul-Ki Jeong,You 한국당과학회 2017 한국당과학회 학술대회 Vol.2017 No.01
Glycoprotein conformations are complex and heterogeneous. Currently, site-specific characterization of glycopeptides is a challenge. We sought to establish an efficient method of N-glycoprotein characterization using mass spectrometry (MS). Using alpha-1-acid glycoprotein (AGP) as a model N-glycoprotein, we identified its tryptic N-glycopeptides and examined the data reproducibility in seven laboratories running different LC−MS/MS platforms. We used three test samples and one blind sample to evaluate instrument performance with entire sample preparation workflow. 165 site-specific N-glycopeptides representative of all N-glycosylation sites were identified from AGP 1 and AGP 2 isoforms. The glycopeptide fragmentations by collision-induced dissociation or higher-energy collisional dissociation (HCD) varied based on the MS analyzer. Orbitrap Elite identified the greatest number of AGP N-glycopeptides, followed by Triple TOF and Q-Exactive Plus. Reproducible generation of oxonium ions, glycancleaved glycopeptide fragment ions, and peptide backbone fragment ions was essential for successful identification. Laboratory proficiency affected the number of identified N-glycopeptides. The relative quantities of the 10 major N-glycopeptide isoforms of AGP detected in four laboratories were compared to assess reproducibility. Quantitative analysis showed that the coefficient of variation was <25% for all test samples. Our analytical protocol yielded identification and quantification of site-specific N-glycopeptide isoforms of AGP from control and disease plasma sample.
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Ji-Hyun Yeom,Eunkyoung Shin,Hanyong Jin,Haifeng Liu,Yongyang Luo,Youngwoo Nam,Minkyung Ryu,Wooseok Song,Heeyoun Chi,Jeongkyu Kim,Kangseok Lee,Jeehyeon Bae 한국공업화학회 2023 Journal of Industrial and Engineering Chemistry Vol.126 No.-
Antibodies are being increasingly used for therapeutic purposes due to their remarkable target specificityand affinity. However, currently available antibody therapies are restricted to target proteins in the outercell membrane or in the extracellular fluids because of the lack of technologies for effective intracellulardelivery of antibodies. Here, we report an efficient and versatile intracellular antibody delivery system. This system is based on gold nanoparticles (AuNPs) conjugated with DNA aptamers (Apt) against theFc region of IgG (AuNP-AptIgG), allowing to load any antibodies onto the AuNP-AptIgG by simple mixing. This AuNP-AptIgG-Ab platform was effective for cytosolic delivery of antibodies to clinically importantmutant proteins via scavenger receptors and caveolae-mediated endocytosis. Specifically, cancer cellsexpressing BRAFV600E, a variant of BRAF identified in numerous types of cancers, exhibited reduced cellviability by 70% when BRAFV600E antibodies were intracellularly delivered using the AuNP-AptIgG(AuNP-AptIgG-aBRAFV600E). In addition, subcutaneous injection of AuNP-AptIgG-aBRAFV600E into in vivoxenografted melanoma tumors expressing BRAFV600E resulted in both inhibition of proliferation andinduction of apoptosis, leading to tumor regression in mice. Thus, our findings indicate that the AuNPAptIgG-Ab system can serve as a promising platform for effective intracellular delivery of antibodies fortherapeutic purposes.
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