An intrinsically stable antibody scFv fragment can tolerate the loss of both disul ¢ de bonds and fold correctly

@inproceedings{Worn1998AnIS,
  title={An intrinsically stable antibody scFv fragment can tolerate the loss of both disul ¢ de bonds and fold correctly},
  author={Arne Wo{\"e}rn and Andreas Plu{\"e}ckthun},
  year={1998}
}
  • Arne Woërn, Andreas Pluëckthun
  • Published 1998
A fully functional cysteine-free derivative of the intrinsically stable anti-HER2 scFv fragment hu4D5^8 was generated by replacing the disulfide forming cysteine residues in VH and VL with the amino acid combination valine-alanine in both domains. The antigen binding properties, determined by ELISA and BIAcore measurements, were not affected by removal of the disulfide bonds. The thermodynamic stability of the disulfide-containing scFv of 8.1 kcal/mol is decreased upon complete reduction of… CONTINUE READING

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