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A comparison of strategies to stabilize immunoglobulin Fv-fragments
Abstract
Fv-Fragments of antibodies may dissociate at low protein concentrations and are too unstable for many applications at physiological temperatures. To stabilize Fv-fragments against dissociation, we have tested and compared three different strategies on the Fv-fragment of the well-characterized phosphocholine binding antibody McPC603 expressed and secreted in Escherichia coli: chemical cross-linking of the variable domains, introduction of an intermolecular disulfide bond, and construction of a peptide linker to produce a "single-chain" Fv-fragment. All the linked fragments show hapten affinities nearly identical with that of the whole antibody independent of protein concentration and are significantly (up to 60-fold) stabilized against irreversible thermal denaturation. All genetically engineered linked Fv-fragments can be obtained in native conformation in E. coli. The reported strategies for generating Fv-fragments with improved physicochemical properties may extend their usefulness in biotechnology as well as in therapeutic and diagnostic applications.
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Citations
Cited by
"Diabodies": small bivalent and bispecific antibody fragments.
Holliger, P., Prospero, T., & Winter, G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6444 · Cited by 874
Properties, production, and applications of camelid single-domain antibody fragments
Harmsen, M. M., & De Haard, H. J. (2007) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-007-1142-2 · Cited by 809
“Such molecules (diabodies, Fig. 1a) can be produced using conventional recombinant antibodies using linkers between the VH and VL domains of a specific length, although this often results in aggregation and reduced affinity because of mispairing of VH and VL domains ( Glockshuber et al. 1990; Whitlow et al. 1993).”
BackgroundKnappik, A., Ge, L., Honegger, A., Pack, P., Fischer, M., Wellnhofer, G., Hoess, A., Wölle, J., Plückthun, A., & Virnekäs, B. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3444 · Cited by 728
Stability engineering of antibody single-chain Fv fragments
Wörn, A., & Plückthun, A. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4265 · Cited by 616
Mack, M., Riethmüller, G., & Kufer, P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.15.7021 · Cited by 351
Metadata
- Authors
- Glockshuber, R., Malia, M., Pfitzinger, I., & Plueckthun, A.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1990-02-13
- Volume
- 29
- Issue
- 6
- Pages
- 1362-1367
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2073517578
- Cited by
- 473
- References
- 0
- FWCI
- 38.54
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: A comparison of strategies to stabilize immunoglobulin Fv-fragments. https://app.cochat.ai/papers/10.1021/bi00458a002
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- Glockshuber, R., Malia, M., Pfitzinger, I., & Plueckthun, A. (1990). A comparison of strategies to stabilize immunoglobulin Fv-fragments. Biochemistry. https://doi.org/10.1021/bi00458a002
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
