Synthesis and characterization of a high-affinity α vβ 6-specific ligand for in vitro and in vivo applications

Shunzi Li, Michael J. McGuire, Mai Lin, Ying Horng Liu, Tsukasa Oyama, Xiankai Sun, Kathlynn C. Brown

Research output: Contribution to journalArticlepeer-review

42 Scopus citations


The α vβ 6 integrin is an attractive therapeutic target for several cancers due to its role in metastasis and its negligible expression in normal tissues. We previously identified a peptide from a phage-displayed peptide library that binds specifically to α vβ 6. The tetrameric version of the peptide has higher affinity for its cellular targets than the corresponding monomers. However, the inefficient synthesis limits its clinical potential. We report here a convergent synthesis producing the tetrameric peptide in high yield and purity. The ease of the synthesis allows for rapid optimization of the peptide. We have optimized this α vβ 6 integrin-binding peptide, determining the minimal binding domain and valency. Importantly, the half-maximal binding affinity of the optimal peptide for its target cell is in the 40 to 60 pmol/L range, rivaling the affinity of commonly used antibody-targeting reagents. This peptide mediates cell-specific uptake, is functional in diagnostic formats, is stable in sera, and can home to a tumor in an animal. We anticipate that this high-affinity ligand for α vβ 6 will find clinical use as a diagnostic and therapeutic reagent.

Original languageEnglish (US)
Pages (from-to)1239-1249
Number of pages11
JournalMolecular Cancer Therapeutics
Issue number5
StatePublished - May 1 2009

ASJC Scopus subject areas

  • Oncology
  • Cancer Research


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