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Domain antibodies: proteins for therapy
Lucy J Holt1, Chris Herring, Laurent S Jespers
1Domantis Limited, Granta Park, Abington, Cambridge CB1 6GS, UK. lucy.holt@domantis.com
Trends in Biotechnology
|October 24, 2003
Summary
Domain antibodies (dAbs) are small, stable antigen-binding fragments derived from heavy chain immunoglobulins. These highly expressed, soluble antibody fragments offer versatile formatting for enhanced drug development.
Area of Science:
- Biotechnology
- Immunology
- Protein Engineering
Background:
- Domain antibodies (dAbs) are naturally occurring fragments of heavy chain immunoglobulins found in camelids.
- They represent the smallest known antigen-binding antibody fragments, with molecular weights between 11 kDa and 15 kDa.
- dAbs are derived from the variable regions of heavy (VH) and light (VL) immunoglobulin chains.
Purpose of the Study:
- To describe the characteristics and potential applications of domain antibodies (dAbs).
- To highlight the advantages of dAbs in biopharmaceutical development.
- To emphasize their suitability for in vitro selection and therapeutic formatting.
Main Methods:
- Production of fully human domain antibodies (dAbs).
- High-level expression in microbial cell culture systems.
- Characterization of biophysical properties, including solubility and thermal stability.
- Application of in vitro selection systems, such as phage display, for affinity maturation.
Main Results:
- Domain antibodies (dAbs) exhibit favorable biophysical properties, including excellent solubility and temperature stability.
- They demonstrate high expression levels in microbial cell cultures.
- dAbs are effective as monomers and can be engineered into larger formats.
Conclusions:
- Domain antibodies (dAbs) are robust, small-sized antibody fragments with significant therapeutic potential.
- Their inherent stability and ease of production make them highly suitable for drug development.
- dAbs can be formatted to achieve prolonged serum half-lives and other desired pharmacological activities.