Difference between revisions of "Part:BBa K5302007:Design"
 
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[2]Pan B, Li B, Russell SJ, Tom JY, Cochran AG, Fairbrother WJ. Solution structure of a phage-derived peptide antagonist in complex with vascular endothelial growth factor. J Mol Biol. 2002 Feb 22;316(3):769-87. doi: 10.1006/jmbi.2001.5370
 
[2]Pan B, Li B, Russell SJ, Tom JY, Cochran AG, Fairbrother WJ. Solution structure of a phage-derived peptide antagonist in complex with vascular endothelial growth factor. J Mol Biol. 2002 Feb 22;316(3):769-87. doi: 10.1006/jmbi.2001.5370
 
[3]Checco JW, Kreitler DF, Thomas NC, Belair DG, Rettko NJ, Murphy WL, Forest KT, Gellman SH. Targeting diverse protein-protein interaction interfaces with α/β-peptides derived from the Z-domain scaffold. Proc Natl Acad Sci U S A. 2015 Apr 14;112(15):4552-7. doi: 10.1073/pnas.1420380112
 
[3]Checco JW, Kreitler DF, Thomas NC, Belair DG, Rettko NJ, Murphy WL, Forest KT, Gellman SH. Targeting diverse protein-protein interaction interfaces with α/β-peptides derived from the Z-domain scaffold. Proc Natl Acad Sci U S A. 2015 Apr 14;112(15):4552-7. doi: 10.1073/pnas.1420380112
−
[3]Checco JW, Gellman SH. Iterative Nonproteinogenic Residue Incorporation Yields α/β-Peptides with a Helix-Loop-Helix Tertiary Structure and High Affinity for VEGF. Chembiochem. 2017 Feb 1;18(3):291-299. doi: 10.1002/cbic.201600545
+
[4]Checco JW, Gellman SH. Iterative Nonproteinogenic Residue Incorporation Yields α/β-Peptides with a Helix-Loop-Helix Tertiary Structure and High Affinity for VEGF. Chembiochem. 2017 Feb 1;18(3):291-299. doi: 10.1002/cbic.201600545

Latest revision as of 12:52, 1 October 2024


V107


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

Please be advised that all listed genes have undergone codon optimization for our chassis strain, Escherichia coli Nissle 1917 (EcN). For those considering alternative chassis organisms, it is recommended to reassess the necessity of codon optimization.


Source

Rational design

References

[1].Ivan Guryanov*, Viktor Korzhikov-Vlakh, Madhushree Bhattacharya, Barbara Biondi, Giulia Masiero, Fernando Formaggio, Tatiana Tennikova, Arto Urtt. Conformationally Constrained Peptides with High Affinity to the Vascular Endothelial Growth Factor.Journal of Medicinal Chemistry. Vol 64/Issue 15.July 16, 2021 [2]Pan B, Li B, Russell SJ, Tom JY, Cochran AG, Fairbrother WJ. Solution structure of a phage-derived peptide antagonist in complex with vascular endothelial growth factor. J Mol Biol. 2002 Feb 22;316(3):769-87. doi: 10.1006/jmbi.2001.5370 [3]Checco JW, Kreitler DF, Thomas NC, Belair DG, Rettko NJ, Murphy WL, Forest KT, Gellman SH. Targeting diverse protein-protein interaction interfaces with α/β-peptides derived from the Z-domain scaffold. Proc Natl Acad Sci U S A. 2015 Apr 14;112(15):4552-7. doi: 10.1073/pnas.1420380112 [4]Checco JW, Gellman SH. Iterative Nonproteinogenic Residue Incorporation Yields α/β-Peptides with a Helix-Loop-Helix Tertiary Structure and High Affinity for VEGF. Chembiochem. 2017 Feb 1;18(3):291-299. doi: 10.1002/cbic.201600545