Affinity-controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled-coil interactions
Long-term delivery is a successful strategy used to reduce the adverse effects of monoclonal antibody (mAb)-based treatments. Macroporous hydrogels and affinity-based strategies have shown promising results in sustained and localized delivery of the mAbs. Among the potential tools for affinity-based...
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2023-12-01
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| Series: | mAbs |
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| Online Access: | https://www.tandfonline.com/doi/10.1080/19420862.2023.2218951 |
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| author | Seyed Farzad Baniahmad Romane Oliverio Ines Obregon-Gomez Alma Robert Anne E.G. Lenferink Elena Pazos Nick Virgilio Xavier Banquy Gregory De Crescenzo Yves Durocher |
| author_facet | Seyed Farzad Baniahmad Romane Oliverio Ines Obregon-Gomez Alma Robert Anne E.G. Lenferink Elena Pazos Nick Virgilio Xavier Banquy Gregory De Crescenzo Yves Durocher |
| author_sort | Seyed Farzad Baniahmad |
| collection | DOAJ |
| description | Long-term delivery is a successful strategy used to reduce the adverse effects of monoclonal antibody (mAb)-based treatments. Macroporous hydrogels and affinity-based strategies have shown promising results in sustained and localized delivery of the mAbs. Among the potential tools for affinity-based delivery systems, the de novo designed Ecoil and Kcoil peptides are engineered to form a high-affinity, heterodimeric coiled-coil complex under physiological conditions. In this study, we created a set of trastuzumab molecules tagged with various Ecoil peptides and evaluated their manufacturability and characteristics. Our data show that addition of an Ecoil tag at the C-termini of the antibody chains (light chains, heavy chains, or both) does not hinder the production of chimeric trastuzumab in CHO cells or affect antibody binding to its antigen. We also evaluated the influence of the number, length, and position of the Ecoil tags on the capture and release of Ecoil-tagged trastuzumab from macroporous dextran hydrogels functionalized with Kcoil peptide (the Ecoil peptide-binding partner). Notably, our data show that antibodies are released from the macroporous hydrogels in a biphasic manner; the first phase corresponding to the rapid release of residual, unbound trastuzumab from the macropores, followed by the affinity-controlled, slow-rate release of antibodies from the Kcoil-functionalized macropore surface. |
| format | Article |
| id | doaj-art-71ba275737b74e2f8835f58cc65a74d4 |
| institution | Kabale University |
| issn | 1942-0862 1942-0870 |
| language | English |
| publishDate | 2023-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | mAbs |
| spelling | doaj-art-71ba275737b74e2f8835f58cc65a74d42025-08-20T03:51:53ZengTaylor & Francis GroupmAbs1942-08621942-08702023-12-0115110.1080/19420862.2023.2218951Affinity-controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled-coil interactionsSeyed Farzad Baniahmad0Romane Oliverio1Ines Obregon-Gomez2Alma Robert3Anne E.G. Lenferink4Elena Pazos5Nick Virgilio6Xavier Banquy7Gregory De Crescenzo8Yves Durocher9Department of Biochemistry and Molecular Medicine, Faculty of Medicine, University of Montreal, Montreal, QC, CanadaDepartment of Chemical Engineering Polytechnique Montréal, Montréal, Québec CanadaCICA - Centro Interdisciplinar de Química E Bioloxía and Departamento de Química, Facultade de Ciencias, Universidade da Coruna, Coruna, SpainHuman Health Therapeutics Research Centre, Building Montreal-Royalmount, National Research Council Canada, Montréal, Québec, CanadaHuman Health Therapeutics Research Centre, Building Montreal-Royalmount, National Research Council Canada, Montréal, Québec, CanadaCICA - Centro Interdisciplinar de Química E Bioloxía and Departamento de Química, Facultade de Ciencias, Universidade da Coruna, Coruna, SpainDepartment of Chemical Engineering, Centre de Recherche Sur Les Systèmes Polymères Et Composites à Haute Performance (CREPEC), Montréal, CanadaFaculty of Pharmacy, Axe Formulation Et Analyse du Médicament, Université de Montréal, Québec, CanadaDepartment of Chemical Engineering Polytechnique Montréal, Montréal, Québec CanadaDepartment of Biochemistry and Molecular Medicine, Faculty of Medicine, University of Montreal, Montreal, QC, CanadaLong-term delivery is a successful strategy used to reduce the adverse effects of monoclonal antibody (mAb)-based treatments. Macroporous hydrogels and affinity-based strategies have shown promising results in sustained and localized delivery of the mAbs. Among the potential tools for affinity-based delivery systems, the de novo designed Ecoil and Kcoil peptides are engineered to form a high-affinity, heterodimeric coiled-coil complex under physiological conditions. In this study, we created a set of trastuzumab molecules tagged with various Ecoil peptides and evaluated their manufacturability and characteristics. Our data show that addition of an Ecoil tag at the C-termini of the antibody chains (light chains, heavy chains, or both) does not hinder the production of chimeric trastuzumab in CHO cells or affect antibody binding to its antigen. We also evaluated the influence of the number, length, and position of the Ecoil tags on the capture and release of Ecoil-tagged trastuzumab from macroporous dextran hydrogels functionalized with Kcoil peptide (the Ecoil peptide-binding partner). Notably, our data show that antibodies are released from the macroporous hydrogels in a biphasic manner; the first phase corresponding to the rapid release of residual, unbound trastuzumab from the macropores, followed by the affinity-controlled, slow-rate release of antibodies from the Kcoil-functionalized macropore surface.https://www.tandfonline.com/doi/10.1080/19420862.2023.2218951AffinityCoiled-coilsHydrogelsMonoclonal antibodiesSustained release |
| spellingShingle | Seyed Farzad Baniahmad Romane Oliverio Ines Obregon-Gomez Alma Robert Anne E.G. Lenferink Elena Pazos Nick Virgilio Xavier Banquy Gregory De Crescenzo Yves Durocher Affinity-controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled-coil interactions mAbs Affinity Coiled-coils Hydrogels Monoclonal antibodies Sustained release |
| title | Affinity-controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled-coil interactions |
| title_full | Affinity-controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled-coil interactions |
| title_fullStr | Affinity-controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled-coil interactions |
| title_full_unstemmed | Affinity-controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled-coil interactions |
| title_short | Affinity-controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled-coil interactions |
| title_sort | affinity controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled coil interactions |
| topic | Affinity Coiled-coils Hydrogels Monoclonal antibodies Sustained release |
| url | https://www.tandfonline.com/doi/10.1080/19420862.2023.2218951 |
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