Novel analogs of VIP with multiple C-terminal domains

David Dangoor, Sara Rubinraut, Mati Fridkin, Illana Gozes

Research output: Contribution to journalArticlepeer-review


The effect of multiplication of the N-terminal domain of vasoactive intestinal peptide (VIP) on the binding activity of the peptide was recently evaluated. A VIP analog with multiple N-terminal domains was found to be slightly more potent as compared to [Nle17]VIP towards VIP receptor type 1 (VPAC1)-related cAMP production. Here, the effect of multiplication of the C-terminal domain of VIP was evaluated with the aim of possibly amplifying peptide-receptor (VPAC1) binding and activation. Several VIP analogs were designed and synthesized, each carrying multiplication of the C-terminal domain that was obtained by either a simple linear tandem extension or by a unique branching methodology. Results show that despite significant alterations in the C-terminal domain of VIP that is considered essential to induce potent receptor binding, few peptides demonstrated only slight reduction in receptor binding and activation in comparison to [Nle17]VIP. Furthermore, a specific branched VIP analog with multiple C-terminal domains was equipotent to [Nle17]VIP in the cAMP production assay. Therefore, it is concluded that the association between the VIP ligand to the VIP receptor could be tolerable to size increases in the C-terminal region of the VIP ligand and multiplication of the C-terminal does not increase activity.

Original languageEnglish
Pages (from-to)1622-1630
Number of pages9
Issue number9
StatePublished - Sep 2007


  • HT-29 cells
  • Peptides
  • Receptor binding
  • VIP
  • VPAC1
  • cAMP


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