The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
The making of bispecific antibodies
Open accessAbstract
During the past two decades we have seen a phenomenal evolution of bispecific antibodies for therapeutic applications. The 'zoo' of bispecific antibodies is populated by many different species, comprising around 100 different formats, including small molecules composed solely of the antigen-binding sites of two antibodies, molecules with an IgG structure, and large complex molecules composed of different antigen-binding moieties often combined with dimerization modules. The application of sophisticated molecular design and genetic engineering has solved many of the technical problems associated with the formation of bispecific antibodies such as stability, solubility and other parameters that confer drug properties. These parameters may be summarized under the term 'developability'. In addition, different 'target product profiles', i.e., desired features of the bispecific antibody to be generated, mandates the need for access to a diverse panel of formats. These may vary in size, arrangement, valencies, flexibility and geometry of their binding modules, as well as in their distribution and pharmacokinetic properties. There is not 'one best format' for generating bispecific antibodies, and no single format is suitable for all, or even most of, the desired applications. Instead, the bispecific formats collectively serve as a valuable source of diversity that can be applied to the development of therapeutics for various indications. Here, a comprehensive overview of the different bispecific antibody formats is provided.
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Cites
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Alternative molecular formats and therapeutic applications for bispecific antibodies
Spiess, C., Zhai, Q., & Carter, P. J. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.01.003 · Cited by 607
Kloepper, J., Riedemann, L., Amoozgar, Z., Seano, G., Susek, K., Yu, V., Dalvie, N., Amelung, R. L., Datta, M., Song, J. W., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1525360113 · Cited by 357
Mack, M., Riethmüller, G., & Kufer, P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.15.7021 · Cited by 351
Bispecific antibodies for cancer therapy: The light at the end of the tunnel?
Chames, P., & Baty, D. (2009) · mAbs · doi:10.4161/mabs.1.6.10015 · Cited by 336
Alt, N., Zhang, T. Y., Motchnik, P., Taticek, R., Quarmby, V., Schlothauer, T., Beck, H., Emrich, T., & Harris, R. J. (2016) · Biologicals · doi:10.1016/j.biologicals.2016.06.005 · Cited by 294
BiTEs: bispecific antibody constructs with unique anti-tumor activity
Wolf, E., Hofmeister, R., Kufer, P., Schlereth, B., & Baeuerle, P. A. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03554-3 · Cited by 260
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“Preferential pairing of light chains with its corresponding heavy chain was described.(141) Importantly, the heteromeric Fc part allows fractionated purification by protein A chromatography”
BackgroundMethodRossi, E. A., Goldenberg, D. M., Cardillo, T. M., McBride, W. J., Sharkey, R. M., & Chang, C.-H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600982103 · Cited by 209
A revival of bispecific antibodies
Kufer, P., Lutterbüse, R., & Baeuerle, P. A. (2004) · Trends in Biotechnology · doi:10.1016/j.tibtech.2004.03.006 · Cited by 157
Cited by
Bispecific antibodies: a mechanistic review of the pipeline
Labrijn, A. F., Janmaat, M. L., Reichert, J. M., & Parren, P. W. H. I. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0028-1 · Cited by 1,303
Nanobodies and nanobody-based human heavy chain antibodies as antitumor therapeutics
Bannas, P., Hambach, J., & Koch-Nolte, F. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01603 · Cited by 572
“Dimerization of two nanobodies or scFvs can also be achieved by genetic fusion to natural or synthetic dimerization domains (56).”
BackgroundBispecific antibodies: design, therapy, perspectives
Sedykh, S., Prinz, V., Buneva, V., & Nevinsky, G. (2018) · Drug Design, Development and Therapy · doi:10.2147/dddt.s151282 · Cited by 292
A review of bispecific antibodies and antibody constructs in oncology and clinical challenges
Suurs, F. V., Lub-de Hooge, M. N., de Vries, E. G. E., & de Groot, D. J. A. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.04.006 · Cited by 292
Bispecific T cell engagers: an emerging therapy for management of hematologic malignancies
Tian, Z., Liu, M., Zhang, Y., & Wang, X. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01084-4 · Cited by 282
Metadata
- Authors
- Brinkmann, U., & Kontermann, R. E.
- Venue
- mAbs
- Publisher
- Informa UK Limited
- Published
- 2017-01-10
- Volume
- 9
- Issue
- 2
- Pages
- 182-212
- ISSN
- 1942-0862 (ISSN-L)
- 1942-0870
- OpenAlex
- W2571138221
- Cited by
- 923
- References
- 12
- FWCI
- 58.31
- Type
- journal article
- Language
- en
- Open access
- gold
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