Improved production of single domain antibodies with two disulfide bonds by co-expression of chaperone proteins in the Escherichia coli periplasm.

@article{ShriverLake2017ImprovedPO,
  title={Improved production of single domain antibodies with two disulfide bonds by co-expression of chaperone proteins in the Escherichia coli periplasm.},
  author={Lisa C. Shriver-Lake and E. R. Goldman and Daniel Zabetakis and George P. Anderson},
  journal={Journal of immunological methods},
  year={2017},
  volume={443},
  pages={64-67}
}
Single domain antibodies are recombinantly expressed variable domains derived from camelid heavy chain antibodies. Natural single domain antibodies can have noncanonical disulfide bonds between their complementarity-determining regions that help position the binding site. In addition, engineering a second disulfide bond serves to tie together β-sheets thereby inhibiting unfolding. Unfortunately, the additional disulfide bond often significantly decreases yield, presumably due to formation of… CONTINUE READING
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