The Product Spotlight: "For Oncology Research, RGD is the VIP"

Even casual followers of this newsletter are probably aware that Peptides International has a comprehensive portfolio and extensive knowledge base of RGD (containing the Arg-Gly-Asp sequence) peptides.  These peptides have been long known to researchers as important tools for NCE (new chemical entities), drug design and development, preparation of radiolabeled derivatives for tumor targeting and imaging, and in novel biomaterials development.  They also play a special role in cell recognition, and related processes such as angiogenesis or endothelial apoptosis.  Design of drugs based on the RGD structure that inhibit the αvβ3 integrin function has been a focus of intense study for developing new treatments for cancer.1


For example, the cyclic pentapeptide cyclo(RGDf(NMe)V),2 CilengitideTM, an inhibitor of αvβ3 and αvβ5 integrin receptors, is being evaluated as a cancer drug3-5and is currently in phase III clinical trials for treatment of glioblastoma multiforme.6

Studies have also indicated that dendrimeric RGD conjugates may enhance the delivery of imaging agents that target carcinoma cells7,8and hold promise for siRNA delivery to solid tumors such as glioma.9

Peptides International has a large variety of RGD peptides for oncology research.  These include:

 Remember that if we don’t have it, we can make it!  Custom peptide synthesis is a specialty, including

  • Chemical route development
  • Process scale-up, multi-gram preparations, pilot-scale synthesis
  • Examples of analogs and derivatives:
    • Cyclic and linear RGD molecules
    • Multivalent peptides (dimeric to octameric)
    • Complex organic hybrids
    • Defined length PEG and bifunctional linkers
    • Biotin, fluorophores and chromophores
    • Chelating agents

Please contact us today for a quote or information on either our catalog or custom RGD products and services.


  1. H.M. Sheldrake and L.H. Patterson, Curr. Cancer Drug Targets, 4, 519 (2009). (Review)
  2. M. A. Dechantsreiter, E. Planker, B. Mathä, E. Lohof, G. Hölzemann, A. Jonczyk, S.L. Goodman, and H. Kessler, J. Med. Chem., 42, 3033 (1999).
  3. J.W. Smith, Curr. Opin. Investig. Drugs, 4, 741 (2003).
  4. D.A. Reardon, K.L. Fink, T. Mikkelsen, T.F. Cloughesy, A. O’Neill, S. Plotkin, M. Glantz, P. Ravin, J.J. Raizer, K.M. Rich, D. Schiff, W.R. Shapiro, S. Burdette-Radoux, E.J. Dropcho, S.M. Wittemer, J. Nippgen, M. Picard, and L.B. Nabors, J. Clin. Oncol., 26, 5610 (2008).
  5.  L. B. Nabors, T. Mikkelsen, T. Batchelor, G. Lesser, M. Rosenfeld, X. Ye, S. Piantadosi, J. Olson, S. Brem, and S. Grossman, J. Clin. Oncol., 27:15s, (suppl; abstr 2001) (2009).
  7. C.A. Boswell, P.K. Eck, C.A. Regino, M. Bernardo, K.J. Wong, D.E. Milenic, P.L. Choyke, and M.W. Brechbiel, Mol. Pharm., 5, 527 (2008).
  8. R. Shukla, T.P. Thomas, J. Peters, A. Kotlyar, A. Myc, and J.R. Baker Jr., Chem. Commun. (Camb.), 5739, DOI: 10.1039/b507350b (2005).
  9. C.L. Waite and C.M. Roth, Bioconjug. Chem., 2009 Sep 23. [Epub ahead of print], PMID: 19775120 (2009).