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Antibody Conjugate

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Franck Denat – One of the best experts on this subject based on the ideXlab platform.

  • DOTAGA-Trastuzumab. A New Antibody Conjugate Targeting HER2/Neu Antigen for Diagnostic Purposes.
    Bioconjugate Chemistry, 2012
    Co-Authors: Mathieu Moreau, Olivier Raguin, Jean-marc Vrigneaud, Bertrand Collin, Claire Bernhard, Xavier Tizon, Frederic Boschetti, Olivier Duchamp, François Brunotte, Franck Denat

    Abstract:

    Improved bifunctional chelating agents (BFC) are required for indium-111 radiolabeling of monoclonal antibodies (mAbs) under mild conditions to yield stable, target-specific agents. 2,2′,2″-(10-(2,6-Dioxotetrahydro-2H-pyran-3-yl)-1,4,7,10-tetraazacyclododecane-1,4,7-triyl)triacetic acid (DOTAGA-anhydride) was evaluated for mAb conjugation and labeling with indium-111. The DOTA analogue was synthesized and Conjugated to trastuzumab-which targets the HER2/neu receptor-in mild conditions (PBS pH 7.4, 25 °C, 30 min) and gave a mean degree of conjugation of 2.6 macrocycle per Antibody. Labeling of this immunoConjugate with indium-111 was performed in 75% yield after 1 h at 37 °C, and the proportion of (111)In-DOTAGA-trastuzumab reached 97% after purification. The affinity of DOTAGA-trastuzumab was 5.5 ± 0.6 nM as evaluated by in vitro saturation assays using HCC1954 breast cancer cell line. SPECT/CT imaging and biodistribution studies were performed in mice bearing breast cancer BT-474 xenografts. BT-474 tumors were clearly visualized on SPECT images at 24, 48, and 72 h postinjection. The tumor uptake of [(111)In-DOTAGA]-trastuzumab reached 65%ID/g 72 h postinjection. These results show that the DOTAGA BFC appears to be a valuable tool for biologics conjugation.

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  • DOTAGA-Trastuzumab. A New Antibody Conjugate Targeting HER2/Neu Antigen for Diagnostic Purposes.
    Bioconjugate Chemistry, 2012
    Co-Authors: Mathieu Moreau, Olivier Raguin, Jean-marc Vrigneaud, Bertrand Collin, Claire Bernhard, Xavier Tizon, Frederic Boschetti, Olivier Duchamp, François Brunotte, Franck Denat

    Abstract:

    Improved bifunctional chelating agents (BFC) are required for indium-111 radiolabeling of monoclonal antibodies (mAbs) under mild conditions to yield stable, target-specific agents. 2,2′,2″-(10-(2,6-Dioxotetrahydro-2H-pyran-3-yl)-1,4,7,10-tetraazacyclododecane-1,4,7-triyl)triacetic acid (DOTAGA-anhydride) was evaluated for mAb conjugation and labeling with indium-111. The DOTA analogue was synthesized and Conjugated to trastuzumab—which targets the HER2/neu receptor—in mild conditions (PBS pH 7.4, 25 °C, 30 min) and gave a mean degree of conjugation of 2.6 macrocycle per Antibody. Labeling of this immunoConjugate with indium-111 was performed in 75% yield after 1 h at 37 °C, and the proportion of 111In-DOTAGA-trastuzumab reached 97% after purification. The affinity of DOTAGA-trastuzumab was 5.5 ± 0.6 nM as evaluated by in vitro saturation assays using HCC1954 breast cancer cell line. SPECT/CT imaging and biodistribution studies were performed in mice bearing breast cancer BT-474 xenografts. BT-474 tumors …

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Rongsheng E Wang – One of the best experts on this subject based on the ideXlab platform.

  • A Switchable Site-Specific Antibody Conjugate.
    ACS chemical biology, 2018
    Co-Authors: Zhigang Lyu, Lei Kang, Zakey Yusuf Buuh, Dawei Jiang, Jeffrey C. Mcguth, Haley L. Wissler, Weibo Cai, Rongsheng E Wang

    Abstract:

    Genetic incorporation of unnatural amino acids (UAAs) provides a unique approach to the synthesis of site-specific Antibody Conjugates that are homogeneous and better defined constructs than random Conjugates. Yet, the yield varies for every Antibody, and the process is costly and time-consuming. We have developed a switchable αGCN4-Fab Conjugate that incorporates UAA p-acetylphenylalanine. The GCN4 peptide is used as a switch, and antibodies fused by GCN4 can direct the αGCN4-Fab Conjugate to target different cancer cells for diagnosis, imaging, or therapeutic treatment. More importantly, this switchable Conjugate demonstrated an impressive potential for pretargeted imaging in vivo. This approach illustrates the utility of an orthogonal switch as a general strategy to endow versatility to a single Antibody Conjugate, which should facilitate the application of UAA-based site-specific Conjugates for a host of biomedical uses in the future.

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  • an immunosuppressive Antibody drug Conjugate
    Journal of the American Chemical Society, 2015
    Co-Authors: Rongsheng E Wang, Brian R Lawson, Ying Wang, Jintang Du, V. Deshmukh, Matthew S Tremblay, Travis S Young, Stephanie A Kazane, Feng Wang, Peter G Schultz

    Abstract:

    We have developed a novel Antibody–drug Conjugate (ADC) that can selectively deliver the Lck inhibitor dasatinib to human T lymphocytes. This ADC is based on a humanized Antibody that selectively binds with high affinity to CXCR4, an antigen that is selectively expressed on hematopoietic cells. The resulting dasatinib–Antibody Conjugate suppresses T-cell-receptor (TCR)-mediated T-cell activation and cytokine expression with low nM EC50 and has minimal effects on cell viability. This ADC may lead to a new class of selective immunosuppressive drugs with improved safety and extend the ADC strategy to the targeted delivery of kinase inhibitors for indications beyond oncology.

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Mathieu Moreau – One of the best experts on this subject based on the ideXlab platform.

  • DOTAGA-Trastuzumab. A New Antibody Conjugate Targeting HER2/Neu Antigen for Diagnostic Purposes.
    Bioconjugate Chemistry, 2012
    Co-Authors: Mathieu Moreau, Olivier Raguin, Jean-marc Vrigneaud, Bertrand Collin, Claire Bernhard, Xavier Tizon, Frederic Boschetti, Olivier Duchamp, François Brunotte, Franck Denat

    Abstract:

    Improved bifunctional chelating agents (BFC) are required for indium-111 radiolabeling of monoclonal antibodies (mAbs) under mild conditions to yield stable, target-specific agents. 2,2′,2″-(10-(2,6-Dioxotetrahydro-2H-pyran-3-yl)-1,4,7,10-tetraazacyclododecane-1,4,7-triyl)triacetic acid (DOTAGA-anhydride) was evaluated for mAb conjugation and labeling with indium-111. The DOTA analogue was synthesized and Conjugated to trastuzumab-which targets the HER2/neu receptor-in mild conditions (PBS pH 7.4, 25 °C, 30 min) and gave a mean degree of conjugation of 2.6 macrocycle per Antibody. Labeling of this immunoConjugate with indium-111 was performed in 75% yield after 1 h at 37 °C, and the proportion of (111)In-DOTAGA-trastuzumab reached 97% after purification. The affinity of DOTAGA-trastuzumab was 5.5 ± 0.6 nM as evaluated by in vitro saturation assays using HCC1954 breast cancer cell line. SPECT/CT imaging and biodistribution studies were performed in mice bearing breast cancer BT-474 xenografts. BT-474 tumors were clearly visualized on SPECT images at 24, 48, and 72 h postinjection. The tumor uptake of [(111)In-DOTAGA]-trastuzumab reached 65%ID/g 72 h postinjection. These results show that the DOTAGA BFC appears to be a valuable tool for biologics conjugation.

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  • DOTAGA-Trastuzumab. A New Antibody Conjugate Targeting HER2/Neu Antigen for Diagnostic Purposes.
    Bioconjugate Chemistry, 2012
    Co-Authors: Mathieu Moreau, Olivier Raguin, Jean-marc Vrigneaud, Bertrand Collin, Claire Bernhard, Xavier Tizon, Frederic Boschetti, Olivier Duchamp, François Brunotte, Franck Denat

    Abstract:

    Improved bifunctional chelating agents (BFC) are required for indium-111 radiolabeling of monoclonal antibodies (mAbs) under mild conditions to yield stable, target-specific agents. 2,2′,2″-(10-(2,6-Dioxotetrahydro-2H-pyran-3-yl)-1,4,7,10-tetraazacyclododecane-1,4,7-triyl)triacetic acid (DOTAGA-anhydride) was evaluated for mAb conjugation and labeling with indium-111. The DOTA analogue was synthesized and Conjugated to trastuzumab—which targets the HER2/neu receptor—in mild conditions (PBS pH 7.4, 25 °C, 30 min) and gave a mean degree of conjugation of 2.6 macrocycle per Antibody. Labeling of this immunoConjugate with indium-111 was performed in 75% yield after 1 h at 37 °C, and the proportion of 111In-DOTAGA-trastuzumab reached 97% after purification. The affinity of DOTAGA-trastuzumab was 5.5 ± 0.6 nM as evaluated by in vitro saturation assays using HCC1954 breast cancer cell line. SPECT/CT imaging and biodistribution studies were performed in mice bearing breast cancer BT-474 xenografts. BT-474 tumors …

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