Difference between revisions of "Part:BBa K1366109"

 
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<partinfo>BBa_K1366109 short</partinfo>
 
<partinfo>BBa_K1366109 short</partinfo>
  
This part allows the production of a recombinant pIII protein linked with a pep42 peptide. This peptide change the tropism of the virus M13 and enables it to bind to a receptor called GRP78 that it is highly present in cancer cells. The binding between pep42 and GRP78 receptor allows the bacteriophage to penetrate the cancer cells and this initiates the transfection of DNA mediated with bacteriophages.
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Pep42 is a cell-penetrating peptide that allows the use of phages as a vehicle for site-directed cancer therapy. In detail, it is a cyclic 13-mer oligopeptide (CTVALPGGYVRVC) that specifically binds to glucose-regulated protein 78 (GRP78) [1]. GRP78 is an intracellular chaperone and a member of the heat shock protein 70 (HSP70) family that provides a protective cellular response against stress conditions. Normal GRP78 expression is maintained at low levels but is upregulated in stress environments and induced in tumor environments. GRP78 overexpression has been reported in a variety of tumors, such as prostate, colon, skin, and breast cancers. This GRP78 overexpression represents a potentially attractive target as it results in the presence of GRP78 molecules on the cell surface of these cancer cells [1].
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This peptide will be linked to the pIII phage coat protein in order to change the tropism of the virus M13. The binding between pep42 and GRP78 receptor will allow the bacteriophage to penetrate the cancer cells.
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Reference:
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[1] Arap, M. A., Lahdenranta, J., Mintz, P. J., Hajitou, A., Sarkis, Á. S., Arap, W., & Pasqualini, R. (2004). Cell surface expression of the stress response chaperone GRP78 enables tumor targeting by circulating ligands. Cancer cell,6(3), 275-284.
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Revision as of 22:27, 17 October 2014

pep42 peptide

Pep42 is a cell-penetrating peptide that allows the use of phages as a vehicle for site-directed cancer therapy. In detail, it is a cyclic 13-mer oligopeptide (CTVALPGGYVRVC) that specifically binds to glucose-regulated protein 78 (GRP78) [1]. GRP78 is an intracellular chaperone and a member of the heat shock protein 70 (HSP70) family that provides a protective cellular response against stress conditions. Normal GRP78 expression is maintained at low levels but is upregulated in stress environments and induced in tumor environments. GRP78 overexpression has been reported in a variety of tumors, such as prostate, colon, skin, and breast cancers. This GRP78 overexpression represents a potentially attractive target as it results in the presence of GRP78 molecules on the cell surface of these cancer cells [1].

This peptide will be linked to the pIII phage coat protein in order to change the tropism of the virus M13. The binding between pep42 and GRP78 receptor will allow the bacteriophage to penetrate the cancer cells.


Reference: [1] Arap, M. A., Lahdenranta, J., Mintz, P. J., Hajitou, A., Sarkis, Á. S., Arap, W., & Pasqualini, R. (2004). Cell surface expression of the stress response chaperone GRP78 enables tumor targeting by circulating ligands. Cancer cell,6(3), 275-284.


Sequence and Features


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]