Difference between revisions of "Part:BBa K5271003:Design"

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===Design Notes===
 
===Design Notes===
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Our preliminary results when it is joined with the HER2 nanobody by a linker, the linker should avoid cysteine residues since it potentially reduces the solubility of the dual targeting nanobody in prokaryotic expression system.
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Our preliminary results when it is joined with the EGFR nanobody by a linker, the linker should avoid cysteine residues since it potentially reduces the solubility of the dual targeting nanobody in prokaryotic expression system.
  
 
===Source===
 
===Source===
  
−
The HER2 specific nanobody is an antigen-binding fragments that are derived from Camelus dromedarius heavy-chain antibodies and have advantageous characteristics compared with mAbs and their derived fragments for in vivo targeting [Hamers-Casterman et al., 1993] The EGFR specific nanobody was isolated from a phage library generated from Llama glama lymphocytes that had been immunized with A431 epidermoid carcinoma cells [Roovers et al., 2007]
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The sequence of the HER2-binding peptide -scrambled was randomly generated and had a same length with the HER2 binding region of Panobody.
  
 
===References===
 
===References===
 +
*Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., ... & Hassabis, D. (2021). Highly accurate protein structure prediction with AlphaFold. nature, 596(7873), 583-589.

Latest revision as of 09:03, 29 September 2024


HER2-binding peptide -scrambled


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

Our preliminary results when it is joined with the EGFR nanobody by a linker, the linker should avoid cysteine residues since it potentially reduces the solubility of the dual targeting nanobody in prokaryotic expression system.

Source

The sequence of the HER2-binding peptide -scrambled was randomly generated and had a same length with the HER2 binding region of Panobody.

References

  • Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., ... & Hassabis, D. (2021). Highly accurate protein structure prediction with AlphaFold. nature, 596(7873), 583-589.