An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly
書誌事項
- 公開日
- 1998-05-15
- 権利情報
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- http://onlinelibrary.wiley.com/termsAndConditions#vor
- DOI
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- 10.1016/s0014-5793(98)00463-3
- 公開者
- Wiley
この論文をさがす
説明
<jats:p>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<jats:italic>V</jats:italic><jats:sub>H</jats:sub>and<jats:italic>V</jats:italic><jats:sub>L</jats:sub>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 both disulfides to 2.7 kcal/mol, while that of the valine‐alanine variant is somewhat higher (about 3.8 kcal/mol). Our results suggest that, in principle, a disulfide‐free fully functional derivative of any scFv can be obtained, as long as the corresponding disulfide‐containing scFv has a high enough thermodynamic stability.</jats:p>
収録刊行物
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- FEBS Letters
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FEBS Letters 427 (3), 357-361, 1998-05-15
Wiley