Difference between revisions of "Part:BBa K404155"

 
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<partinfo>BBa_K404155 short</partinfo>
 
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<h2>Affibody Z-EGFR-1907</h2> (BBa_K404302)<br>
 +
Affibodies are small (6 kDa), soluble high-affinity proteins. They are derived from the IgG-binding B domain of the Staphylococcal protein A, which was engineered to specifically bind to certain peptides or proteins. This so-called Z domain consists of an antiparallel three-helix bundle and is advantageous due to its proteolytic and thermodynamic stability, its good folding properties and the ease of production via recombinant bacteria (Nord et al., 1997). Affibodies can be used for example for tumor targeting (Wikman et al., 2004) and diagnostic imaging applications (Orlova et al., 2006; Orlova et al., 2007). The ZEGFR:1907 Affibody was engineered to specifically bind the EGF receptor with an affinity determined to be KD = 2.8 nM (Friedman et al., 2008).
 +
The EGF receptor is overexpressed in certain types of tumors, e.g. in breast (Walker & Dearing, 1999), lung (Hirsch et al., 2003) and bladder (Colquhoun & Mellon, 2002) carcinomas, and is therefore a suitable target for cancer imaging or therapeutic applications. Because of their good tumor uptake, and their property to become internalized into the target cells with an efficiency of 19 – 24% within one hour – compared to 45% of the natural ligand EGF - the ZEGFR:1907 Affibody was chosen for therapeutic applications by the Freiburg iGEM Team 2010 (Friedman et al., 2008; Göstring et al., 2010).
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<partinfo>BBa_K404155 parameters</partinfo>
 
<partinfo>BBa_K404155 parameters</partinfo>
 
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 +
<br>
 +
<br><h2>References</h2>
 +
Mellon. 2002. Epidermal growth factor receptor and bladder cancer.Postgraduate
 +
medical journal78, no. 924 (October): 584-9.
 +
doi:10.1136/pmj.78.924.584.
 +
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1742539&amp;tool=pmcentrez&amp;rendertype=abstract.<br>
 +
Friedman,
 +
Mikaela, Anna
 +
Orlova, Eva Johansson, Tove L J Eriksson, Ingmarie Höidén-Guthenberg,
 +
Vladimir
 +
Tolmachev, Fredrik Y Nilsson, and Stefan Ståhl. 2008. Directed
 +
evolution to low
 +
nanomolar affinity of a tumor-targeting epidermal growth factor
 +
receptor-binding affibody molecule. Journal of molecular
 +
biology376,
 +
no. 5: 1388-402. doi:10.1016/j.jmb.2007.12.060.
 +
http://www.ncbi.nlm.nih.gov/pubmed/18207161.<br>
 +
Göstring,
 +
Lovisa, Ming Tsuey
 +
Chew, Anna Orlova, Ingmarie Höidén-guthenberg, Anders Wennborg, Jörgen
 +
Carlsson, and Fredrik Y Frejd. 2010. Quantification of internalization
 +
of
 +
EGFR-binding Affibody molecules: Methodological aspects. International
 +
Journal of Oncology 36, no. 4 (March): 757-763.
 +
doi:10.3892/ijo_00000551.
 +
http://www.spandidos-publications.com/ijo/36/4/757.<br>
 +
Hirsch,Fred R, Marileila Varella-Garcia, Paul a Bunn, Michael V Di Maria, Robert Veve, Roy M Bremmes,
 +
Anna E Barón, Chan Zeng, and Wilbur a Franklin. 2003. Epidermal growth factor
 +
receptor in non-small-cell lung carcinomas: correlation between gene copy number and protein expression and impact on prognosis. Journal of clinical oncology : official journal of the American Society of Clinical Oncology
 +
21, no. 20 (October): 3798-807. doi:10.1200/JCO.2003.11.069.
 +
http://www.ncbi.nlm.nih.gov/pubmed/12953099.<br>
 +
Nord, K, E Gunneriusson, J Ringdahl, S Ståhl, M Uhlén, and P A Nygren. 1997. Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain. Nature biotechnology 15, no. 8 (August): 772-7. doi:10.1038/nbt0897-772. http://www.ncbi.nlm.nih.gov/pubmed/9255793.<br>
 +
Orlova,
 +
Anna, Vladimir
 +
Tolmachev, Rikard Pehrson, Malin Lindborg, Thuy Tran, Mattias
 +
Sandström,
 +
Fredrik Y Nilsson, Anders Wennborg, Lars Abrahmsén, and Joachim
 +
Feldwisch.
 +
2007. Synthetic affibody molecules: a novel class of affinity ligands
 +
for
 +
molecular imaging of HER2-expressing malignant tumors. Cancer
 +
research
 +
67, no. 5 (March): 2178-86. doi:10.1158/0008-5472.CAN-06-2887.
 +
http://www.ncbi.nlm.nih.gov/pubmed/17332348.<br>
 +
Walker,
 +
R a, and S J Dearing.
 +
1999. Expression of epidermal growth factor receptor mRNA and protein
 +
in
 +
primary breast carcinomas. Breast cancer research and
 +
treatment53, no.
 +
2 (January): 167-76. http://www.ncbi.nlm.nih.gov/pubmed/10326794.<br>
 +
Wikman,
 +
M, a-C Steffen, E
 +
Gunneriusson, V Tolmachev, G P Adams, J Carlsson, and S Ståhl. 2004.
 +
Selection
 +
and characterization of HER2/neu-binding affibody ligands. Protein
 +
engineering, design &amp; selection : PEDS 17, no. 5
 +
(May): 455-62.
 +
doi:10.1093/protein/gzh053. http://www.ncbi.nlm.nih.gov/pubmed/15208403.<br>
 +
&nbsp;<br>

Revision as of 22:08, 27 October 2010

pCMV_Z-EGFR-1907_Short-Linker_[AAV2]-VP23 (ViralBrick-587KO-Empty)

Affibody Z-EGFR-1907

(BBa_K404302)

Affibodies are small (6 kDa), soluble high-affinity proteins. They are derived from the IgG-binding B domain of the Staphylococcal protein A, which was engineered to specifically bind to certain peptides or proteins. This so-called Z domain consists of an antiparallel three-helix bundle and is advantageous due to its proteolytic and thermodynamic stability, its good folding properties and the ease of production via recombinant bacteria (Nord et al., 1997). Affibodies can be used for example for tumor targeting (Wikman et al., 2004) and diagnostic imaging applications (Orlova et al., 2006; Orlova et al., 2007). The ZEGFR:1907 Affibody was engineered to specifically bind the EGF receptor with an affinity determined to be KD = 2.8 nM (Friedman et al., 2008). The EGF receptor is overexpressed in certain types of tumors, e.g. in breast (Walker & Dearing, 1999), lung (Hirsch et al., 2003) and bladder (Colquhoun & Mellon, 2002) carcinomas, and is therefore a suitable target for cancer imaging or therapeutic applications. Because of their good tumor uptake, and their property to become internalized into the target cells with an efficiency of 19 – 24% within one hour – compared to 45% of the natural ligand EGF - the ZEGFR:1907 Affibody was chosen for therapeutic applications by the Freiburg iGEM Team 2010 (Friedman et al., 2008; Göstring et al., 2010).


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 2183
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 665
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 2709
    Illegal SapI site found at 1620




References

Mellon. 2002. Epidermal growth factor receptor and bladder cancer.Postgraduate medical journal78, no. 924 (October): 584-9. doi:10.1136/pmj.78.924.584. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1742539&tool=pmcentrez&rendertype=abstract.
Friedman, Mikaela, Anna Orlova, Eva Johansson, Tove L J Eriksson, Ingmarie Höidén-Guthenberg, Vladimir Tolmachev, Fredrik Y Nilsson, and Stefan Ståhl. 2008. Directed evolution to low nanomolar affinity of a tumor-targeting epidermal growth factor receptor-binding affibody molecule. Journal of molecular biology376, no. 5: 1388-402. doi:10.1016/j.jmb.2007.12.060. http://www.ncbi.nlm.nih.gov/pubmed/18207161.
Göstring, Lovisa, Ming Tsuey Chew, Anna Orlova, Ingmarie Höidén-guthenberg, Anders Wennborg, Jörgen Carlsson, and Fredrik Y Frejd. 2010. Quantification of internalization of EGFR-binding Affibody molecules: Methodological aspects. International Journal of Oncology 36, no. 4 (March): 757-763. doi:10.3892/ijo_00000551. http://www.spandidos-publications.com/ijo/36/4/757.
Hirsch,Fred R, Marileila Varella-Garcia, Paul a Bunn, Michael V Di Maria, Robert Veve, Roy M Bremmes, Anna E Barón, Chan Zeng, and Wilbur a Franklin. 2003. Epidermal growth factor receptor in non-small-cell lung carcinomas: correlation between gene copy number and protein expression and impact on prognosis. Journal of clinical oncology : official journal of the American Society of Clinical Oncology 21, no. 20 (October): 3798-807. doi:10.1200/JCO.2003.11.069. http://www.ncbi.nlm.nih.gov/pubmed/12953099.
Nord, K, E Gunneriusson, J Ringdahl, S Ståhl, M Uhlén, and P A Nygren. 1997. Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain. Nature biotechnology 15, no. 8 (August): 772-7. doi:10.1038/nbt0897-772. http://www.ncbi.nlm.nih.gov/pubmed/9255793.
Orlova, Anna, Vladimir Tolmachev, Rikard Pehrson, Malin Lindborg, Thuy Tran, Mattias Sandström, Fredrik Y Nilsson, Anders Wennborg, Lars Abrahmsén, and Joachim Feldwisch. 2007. Synthetic affibody molecules: a novel class of affinity ligands for molecular imaging of HER2-expressing malignant tumors. Cancer research 67, no. 5 (March): 2178-86. doi:10.1158/0008-5472.CAN-06-2887. http://www.ncbi.nlm.nih.gov/pubmed/17332348.
Walker, R a, and S J Dearing. 1999. Expression of epidermal growth factor receptor mRNA and protein in primary breast carcinomas. Breast cancer research and treatment53, no. 2 (January): 167-76. http://www.ncbi.nlm.nih.gov/pubmed/10326794.
Wikman, M, a-C Steffen, E Gunneriusson, V Tolmachev, G P Adams, J Carlsson, and S Ståhl. 2004. Selection and characterization of HER2/neu-binding affibody ligands. Protein engineering, design & selection : PEDS 17, no. 5 (May): 455-62. doi:10.1093/protein/gzh053. http://www.ncbi.nlm.nih.gov/pubmed/15208403.