Optimal charged mutations in the complementarity-determining regions that prevent domain antibody aggregation are dependent on the antibody scaffold.

Abstract

Therapeutic antibodies need to be highly resistant to aggregation due to the high concentrations required for subcutaneous delivery and the potential immunogenicity of antibody aggregates. Human antibody fragments-such as single-domain antibodies (VH or VL)-are typically much less soluble than full-length antibodies. Nevertheless, some aggregation-resistant… (More)
DOI: 10.1093/protein/gzt058

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Cite this paper

@article{Perchiacca2014OptimalCM, title={Optimal charged mutations in the complementarity-determining regions that prevent domain antibody aggregation are dependent on the antibody scaffold.}, author={Joseph M Perchiacca and Christine P C Lee and Peter M Tessier}, journal={Protein engineering, design & selection : PEDS}, year={2014}, volume={27 2}, pages={29-39} }