Stability engineering of antibody single-chain Fv fragments
Abstract
The application of single-chain Fv fragments (scFv) in medicine and biotechnology places great demands on their stability. Only recently has attention been given to the production of highly stable scFvs, and in a number of examples it was found that such fragments indeed perform better during practical applications. The structural parameters influencing scFv stability are now beginning to be elucidated. This review summarizes progress in rational and evolutionary engineering methods, the structural implications of these results, as well as some examples where stability engineering has been successfully applied.
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In the presence of short linkers, one antibody fragment's VL or VH domain interacts with another molecule's complementary domain through domain swapping, generating dimers or higher-order oligomers.
“In the presence of short linkers, one antibody fragment’s VL or VH domain interacts with another molecule’s complimentary domain through a mechanism known as “domain swapping” generating dimers or higher-order oligomers [21].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [21]
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“In the presence of short linkers, one antibody fragment’s VL or VH domain interacts with another molecule’s complimentary domain through a mechanism known as “domain swapping” generating dimers or higher-order oligomers [21].”
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- Authors
- Wörn, A., & Plückthun, A.
- Affiliations
- University of Zurich (CH)
- Corresponding author
- Plückthun, Andreas
- ORCID
- Plückthun, Andreas
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2001-02
- Volume
- 305
- Issue
- 5
- Pages
- 989-1010
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2022228265
- Cited by
- 616
- References
- 0
- Citations by year
- 2026: 13 · 2025: 15 · 2024: 21 · 2023: 20 · 2022: 16 · 2021: 17 · 2020: 21 · 2019: 14 · 2018: 21 · 2017: 29 · 2016: 34 · 2015: 19 · 2014: 35 · 2013: 28 · 2012: 31
- FWCI
- 5.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- single-chain Fv fragments, antibody fragments, protein stability, rational design, evolutionary engineering, structural parameters, antibody engineering
- MeSH terms
- Animals, Binding Sites, Disulfides, Humans, Immunoglobulin Variable Region, Mutation, Thermodynamics, Protein Engineering, Protein Structure, Tertiary, Directed Molecular Evolution, Peptide Library, Complementarity Determining Regions
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