OhioMod2013:Design: Difference between revisions

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*Use cationic NLS peptide sequences to bind to origami structure.  
*Use cationic NLS peptide sequences to bind to origami structure.  
*NF-kB binding sites demonstrate increased expression in calcium phosphate transfected cells. Zeich's lab also showed that a hydrophobic coat alteration to a protein resulted in its ability to cross the NPC <cite>Reich</cite>.
*NF-kB binding sites demonstrate increased expression in calcium phosphate transfected cells. Zeich's lab also showed that a hydrophobic coat alteration to a protein resulted in its ability to cross the NPC <cite>Reich</cite>.
References
<biblio>
#Reich pmid=19680225
</biblio>

Revision as of 18:15, 14 May 2013

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Design

Cell specificity

Anti-CD71 targets the transferrin receptors of common breast cancer.

For anti-cancer

  • Antibodies targeting EGFRVIII, VEGFR,
  • Folate
  • RGD peptides - target alphaV integrins of the tumour vasculature.

For tissue specificity

  • Use G-protein coupled receptor peptide ligand agonists.

In general, uptake into the cell can be improved by taking advantage of the cellular need to uptake iron (transferrin), folate, EGF, and other factors.

Nuclear pore entry

The origami may be tagged with various sequences or peptides in order to encourage nuclear envelope entry.

  • SV40 72 bp sequence
  • Use cationic NLS peptide sequences to bind to origami structure.
  • NF-kB binding sites demonstrate increased expression in calcium phosphate transfected cells. Zeich's lab also showed that a hydrophobic coat alteration to a protein resulted in its ability to cross the NPC [1].


References

  1. Naim B, Zbaida D, Dagan S, Kapon R, and Reich Z. Cargo surface hydrophobicity is sufficient to overcome the nuclear pore complex selectivity barrier. EMBO J. 2009 Sep 16;28(18):2697-705. DOI:10.1038/emboj.2009.225 | PubMed ID:19680225 | HubMed [Reich]