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  1. Article ; Online: Crotamine-based recombinant immunotoxin targeting HER2 for enhanced cancer cell specificity and cytotoxicity.

    Jang, Jaepyeong / Nguyen, Minh Quan / Park, Sangsu / Ryu, Dayoung / Park, Hyeseon / Lee, Gunsup / Kim, Chong Jai / Jang, Yeon Jin / Choe, Han

    Toxicon : official journal of the International Society on Toxinology

    2023  Volume 230, Page(s) 107157

    Abstract: Crotamine, one of the major toxins present in the venom of the South American rattlesnake Crotalus durissus terrificus, exhibits potent cytotoxic properties and has been suggested for cancer therapy applications. However, its selectivity for cancer cells ...

    Abstract Crotamine, one of the major toxins present in the venom of the South American rattlesnake Crotalus durissus terrificus, exhibits potent cytotoxic properties and has been suggested for cancer therapy applications. However, its selectivity for cancer cells needs to be improved. This study designed and produced a novel recombinant immunotoxin, HER2(scFv)-CRT, composed of crotamine and single-chain Fv (scFv) derived from trastuzumab targeting human epidermal growth factor receptor 2 (HER2). The recombinant immunotoxin was expressed in Escherichia coli and purified using various chromatographic techniques. The cytotoxicity of HER2(scFv)-CRT was assessed in three breast cancer cell lines, demonstrating enhanced specificity and toxicity in HER2-expressing cells. These findings suggest that the crotamine-based recombinant immunotoxin has the potential to expand the repertoire of recombinant immunotoxin applications in cancer therapy.
    MeSH term(s) Animals ; Humans ; Crotalid Venoms/chemistry ; Crotalus ; Immunotoxins/metabolism ; Neoplasms/drug therapy ; Cell Line, Tumor
    Chemical Substances Crotalid Venoms ; crotamine (E58TBP78IH) ; Immunotoxins
    Language English
    Publishing date 2023-05-15
    Publishing country England
    Document type Journal Article
    ZDB-ID 204479-1
    ISSN 1879-3150 ; 0041-0101
    ISSN (online) 1879-3150
    ISSN 0041-0101
    DOI 10.1016/j.toxicon.2023.107157
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Soluble Prokaryotic Expression and Purification of Bioactive Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand.

    Do, Bich Hang / Nguyen, Minh Tan / Song, Jung-A / Park, Sangsu / Yoo, Jiwon / Jang, Jaepyeong / Lee, Sunju / So, Seoungjun / Yoon, Yejin / Kim, Inki / Lee, Kyungjin / Jang, Yeon Jin / Choe, Han

    Journal of microbiology and biotechnology

    2018  Volume 27, Issue 12, Page(s) 2156–2164

    Abstract: Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is considered as an antitumor agent owing to its ability to induce apoptosis of cancer cells without imparting toxicity toward most normal cells. TRAIL is produced in poor yield because of ... ...

    Abstract Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is considered as an antitumor agent owing to its ability to induce apoptosis of cancer cells without imparting toxicity toward most normal cells. TRAIL is produced in poor yield because of its insoluble expression in the cytoplasm of
    MeSH term(s) Antineoplastic Agents/pharmacology ; Apoptosis ; Chromatography, Affinity ; Escherichia coli/genetics ; Escherichia coli/metabolism ; HeLa Cells ; Humans ; Maltose-Binding Proteins/genetics ; Protein Disulfide-Isomerases/genetics ; Solubility ; TNF-Related Apoptosis-Inducing Ligand/biosynthesis ; TNF-Related Apoptosis-Inducing Ligand/genetics
    Chemical Substances Antineoplastic Agents ; Maltose-Binding Proteins ; TNF-Related Apoptosis-Inducing Ligand ; Protein Disulfide-Isomerases (EC 5.3.4.1)
    Language English
    Publishing date 2018-01-11
    Publishing country Korea (South)
    Document type Journal Article
    ISSN 1738-8872
    ISSN (online) 1738-8872
    DOI 10.4014/jmb.1705.05070
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Prokaryotic soluble overexpression and purification of oncostatin M using a fusion approach and genetically engineered E. coli strains.

    Nguyen, Minh Tan / Prima, Musharrat Jahan / Song, Jung-A / Kim, Julee / Do, Bich Hang / Yoo, Jiwon / Park, Sangsu / Jang, Jaepyeong / Lee, Sunju / Lee, Eunyoung / Novais, Michelle de Paula / Seo, Hyeon-Beom / Lee, Seon-Yeong / Cho, Mi-La / Kim, Chong Jai / Jang, Yeon Jin / Choe, Han

    Scientific reports

    2019  Volume 9, Issue 1, Page(s) 13706

    Abstract: Human Oncostatin M (OSM), initially discovered as a tumour inhibitory factor secreted from U-937 cells, is a gp130 (IL-6/LIF) cytokine family member that exhibits pleiotropic effects in inflammation, haematopoiesis, skeletal tissue alteration, liver ... ...

    Abstract Human Oncostatin M (OSM), initially discovered as a tumour inhibitory factor secreted from U-937 cells, is a gp130 (IL-6/LIF) cytokine family member that exhibits pleiotropic effects in inflammation, haematopoiesis, skeletal tissue alteration, liver regeneration, cardiovascular and metabolic diseases. Cytoplasmic expression of OSM in Escherichia coli results in inclusion bodies, and complex solubilisation, refolding and purification is required to prepare bioactive protein. Herein, eight N-terminal fusion variants of OSM with hexahistidine (His6) tag and seven solubility-enhancing tags, including thioredoxin (Trx), small ubiquitin-related modifier (Sumo), glutathione S-transferase (GST), maltose-binding protein (MBP), N-utilisation substance protein A (Nusa), human protein disulphide isomerase (PDI) and the b'a' domain of PDI (PDIb'a'), were tested for soluble OSM expression in E. coli. The His6-OSM plasmid was also introduced into genetically engineered Origami 2 and SHuffle strains to test expression of the protein. At 18 °C, MBP-tagged OSM was highly expressed and solubility was dramatically enhanced. In addition, His6-OSM was more highly expressed and soluble in Origami 2 and SHuffle strains than in BL21(DE3). MBP-OSM and His6-OSM were purified more than 95% with yields of 11.02 mg and 3.27 mg from a 500 mL culture. Protein identity was confirmed by mass spectroscopy, and bioactivity was demonstrated by in vitro inhibition of Th17 cell differentiation.
    MeSH term(s) Escherichia coli ; Gene Expression ; Genetic Engineering ; Histidine ; Humans ; Maltose-Binding Proteins/metabolism ; Oligopeptides ; Oncostatin M/genetics ; Oncostatin M/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Solubility
    Chemical Substances His-His-His-His-His-His ; Maltose-Binding Proteins ; Oligopeptides ; Recombinant Fusion Proteins ; Oncostatin M (106956-32-5) ; Histidine (4QD397987E)
    Language English
    Publishing date 2019-09-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-019-50110-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Granulocyte colony-stimulating factor (GCSF) fused with Fc Domain produced from E. coli is less effective than Polyethylene Glycol-conjugated GCSF.

    Do, Bich Hang / Kang, Hyo Jeong / Song, Jung-A / Nguyen, Minh Tan / Park, Sangsu / Yoo, Jiwon / Nguyen, Anh Ngoc / Kwon, Grace G / Jang, Jaepyeong / Jang, Mihee / Lee, Sunju / So, Seoungjun / Sim, Seongrak / Lee, Kyung Jin / Osborn, Mark J / Choe, Han

    Scientific reports

    2017  Volume 7, Issue 1, Page(s) 6480

    Abstract: Human granulocyte colony-stimulating factor (GCSF) is a well-known cytokine for neutropenia treatment. However, daily injections are required due to the short circulating half-life of the protein. To overcome this bottleneck, we fused GCSF with the Fc ... ...

    Abstract Human granulocyte colony-stimulating factor (GCSF) is a well-known cytokine for neutropenia treatment. However, daily injections are required due to the short circulating half-life of the protein. To overcome this bottleneck, we fused GCSF with the Fc domain of IgG1 at the C terminus (GCSF-Fc) and with the maltose binding protein (MBP) tag at the N-terminus and expressed it as a soluble protein in the cytoplasm of E. coli. We also conjugated PEG aldehyde to GCSF to make PEG-GCSF. The bioactivities of GCSF-Fc and PEG-GCSF were similar to native GCSF using the mouse M-NFS-60 myelogenous leukemia cell line. The EC
    MeSH term(s) Animals ; Cell Line ; Cell Proliferation/drug effects ; Escherichia coli/genetics ; Granulocyte Colony-Stimulating Factor/genetics ; Granulocyte Colony-Stimulating Factor/pharmacology ; Humans ; Hydrogen-Ion Concentration ; Immunoglobulin Fc Fragments/genetics ; Neutropenia/drug therapy ; Polyethylene Glycols/chemistry ; Polyethylene Glycols/pharmacology ; Protein Engineering/methods ; Rats, Sprague-Dawley ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/pharmacology
    Chemical Substances Immunoglobulin Fc Fragments ; Recombinant Proteins ; Granulocyte Colony-Stimulating Factor (143011-72-7) ; Polyethylene Glycols (3WJQ0SDW1A)
    Language English
    Publishing date 2017-07-25
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-017-06726-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Prokaryotic soluble expression and purification of bioactive human fibroblast growth factor 21 using maltose-binding protein.

    Nguyen, Anh Ngoc / Song, Jung-A / Nguyen, Minh Tan / Do, Bich Hang / Kwon, Grace G / Park, Sang Su / Yoo, Jiwon / Jang, Jaepyeong / Jin, Jonghwa / Osborn, Mark J / Jang, Yeon Jin / Thi Vu, Thu Trang / Oh, Heung-Bum / Choe, Han

    Scientific reports

    2017  Volume 7, Issue 1, Page(s) 16139

    Abstract: Human fibroblast growth factor 21 (hFGF21) has been characterized as an important regulator of glucose and lipid metabolism homeostasis. Here, to produce hFGF21 efficiently in Escherichia coli, the expression and solubility of hFGF21 were tested and ... ...

    Abstract Human fibroblast growth factor 21 (hFGF21) has been characterized as an important regulator of glucose and lipid metabolism homeostasis. Here, to produce hFGF21 efficiently in Escherichia coli, the expression and solubility of hFGF21 were tested and optimised by fusing the protein with one of eight tags: hexahistidine (His6), thioredoxin (Trx), small ubiquitin-related modifier (Sumo), glutathione S-transferase (GST), maltose-binding protein (MBP), N-utilisation substance protein A (NusA), human protein disulphide isomerase (PDI), and the b'a' domain of PDI (PDIb'a'). Each tag increased solubility of the protein when the expression temperature was 18°C. Unlike many other tags that were tested, MBP significantly enhanced the solubility of the protein also in the culture condition at 37°C. Thus, the MBP-hFGF21 construct was further pursued for optimisation of affinity chromatography purification. After tag removal, 8.1 mg of pure hFGF21 was obtained as a final product from 500 mL of starting culture. The protein was then characterised by mass spectroscopy and an in vitro functional assay using NIH-3T3 cells transfected with a β-klotho reporter gene. These characteristics are similar to those of commercial hFGF21. Thus, the MBP tag is useful for efficient prokaryotic production and purification of bioactive hFGF21.
    MeSH term(s) Escherichia coli/metabolism ; Fibroblast Growth Factors/genetics ; Fibroblast Growth Factors/metabolism ; Humans ; Maltose-Binding Proteins/genetics ; Maltose-Binding Proteins/metabolism ; Prokaryotic Cells/metabolism ; Protein Disulfide-Isomerases/genetics ; Protein Disulfide-Isomerases/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Thioredoxins/genetics ; Thioredoxins/metabolism
    Chemical Substances Maltose-Binding Proteins ; Recombinant Fusion Proteins ; fibroblast growth factor 21 ; Thioredoxins (52500-60-4) ; Fibroblast Growth Factors (62031-54-3) ; Protein Disulfide-Isomerases (EC 5.3.4.1)
    Language English
    Publishing date 2017-11-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-017-16167-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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