Biophysical and biochemical characterization of a VHH-based IgG-like bi- and trispecific antibody platform
Here, we report the characterization of a VHH-derived IgG-like bi- and trispecific antibody platform that essentially relies on the replacement of the VH and VL regions of a conventional antibody by two independently functioning VHH domains. Consequently, a VHH is engrafted onto constant region CH1...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2020-01-01
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| Series: | mAbs |
| Subjects: | |
| Online Access: | https://www.tandfonline.com/doi/10.1080/19420862.2020.1812210 |
| _version_ | 1828408172118802432 |
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| author | Lukas Pekar Michael Busch Bernhard Valldorf Steffen C. Hinz Lars Toleikis Simon Krah Stefan Zielonka |
| author_facet | Lukas Pekar Michael Busch Bernhard Valldorf Steffen C. Hinz Lars Toleikis Simon Krah Stefan Zielonka |
| author_sort | Lukas Pekar |
| collection | DOAJ |
| description | Here, we report the characterization of a VHH-derived IgG-like bi- and trispecific antibody platform that essentially relies on the replacement of the VH and VL regions of a conventional antibody by two independently functioning VHH domains. Consequently, a VHH is engrafted onto constant region CH1 while the other VHH-based paratope is engrafted on the constant region of the light chain, Cκ or Cλ, resulting in a tetravalent bispecific IgG-like molecule. Combined with a heavy chain heterodimerization technique, this platform allows facile engineering of bi- and trispecific antibodies with flexible valencies. We demonstrate the general applicability of this generic platform approach and elaborate on the limitations of specific formats. |
| first_indexed | 2024-12-10T11:34:47Z |
| format | Article |
| id | doaj.art-8401a02b7d7d4bcf96189b469880f51b |
| institution | Directory Open Access Journal |
| issn | 1942-0862 1942-0870 |
| language | English |
| last_indexed | 2024-12-10T11:34:47Z |
| publishDate | 2020-01-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | mAbs |
| spelling | doaj.art-8401a02b7d7d4bcf96189b469880f51b2022-12-22T01:50:28ZengTaylor & Francis GroupmAbs1942-08621942-08702020-01-0112110.1080/19420862.2020.1812210Biophysical and biochemical characterization of a VHH-based IgG-like bi- and trispecific antibody platformLukas Pekar0Michael Busch1Bernhard Valldorf2Steffen C. Hinz3Lars Toleikis4Simon Krah5Stefan Zielonka6Institute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Darmstadt, GermanyDiscovery Pharmacology, Merck KGaA, Darmstadt, GermanyChemical and Pharmaceutical Development, Merck KGaA, Darmstadt, GermanyInstitute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Darmstadt, GermanyProtein Engineering and Antibody Technologies, Merck KGaA, Darmstadt, GermanyProtein Engineering and Antibody Technologies, Merck KGaA, Darmstadt, GermanyProtein Engineering and Antibody Technologies, Merck KGaA, Darmstadt, GermanyHere, we report the characterization of a VHH-derived IgG-like bi- and trispecific antibody platform that essentially relies on the replacement of the VH and VL regions of a conventional antibody by two independently functioning VHH domains. Consequently, a VHH is engrafted onto constant region CH1 while the other VHH-based paratope is engrafted on the constant region of the light chain, Cκ or Cλ, resulting in a tetravalent bispecific IgG-like molecule. Combined with a heavy chain heterodimerization technique, this platform allows facile engineering of bi- and trispecific antibodies with flexible valencies. We demonstrate the general applicability of this generic platform approach and elaborate on the limitations of specific formats.https://www.tandfonline.com/doi/10.1080/19420862.2020.1812210Antibody engineeringbispecific antibodycamelidIgG-likenanobodysingle-domain antibody |
| spellingShingle | Lukas Pekar Michael Busch Bernhard Valldorf Steffen C. Hinz Lars Toleikis Simon Krah Stefan Zielonka Biophysical and biochemical characterization of a VHH-based IgG-like bi- and trispecific antibody platform mAbs Antibody engineering bispecific antibody camelid IgG-like nanobody single-domain antibody |
| title | Biophysical and biochemical characterization of a VHH-based IgG-like bi- and trispecific antibody platform |
| title_full | Biophysical and biochemical characterization of a VHH-based IgG-like bi- and trispecific antibody platform |
| title_fullStr | Biophysical and biochemical characterization of a VHH-based IgG-like bi- and trispecific antibody platform |
| title_full_unstemmed | Biophysical and biochemical characterization of a VHH-based IgG-like bi- and trispecific antibody platform |
| title_short | Biophysical and biochemical characterization of a VHH-based IgG-like bi- and trispecific antibody platform |
| title_sort | biophysical and biochemical characterization of a vhh based igg like bi and trispecific antibody platform |
| topic | Antibody engineering bispecific antibody camelid IgG-like nanobody single-domain antibody |
| url | https://www.tandfonline.com/doi/10.1080/19420862.2020.1812210 |
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