Multivalent RGD synthetic peptides as potent alphaVbeta3 integrin ligands

Org Biomol Chem. 2006 May 21;4(10):1958-65. doi: 10.1039/b517706e. Epub 2006 Apr 3.

Abstract

We study herein the multivalency effect of a cluster of alphaVbeta3-ligands held on a cyclodecapeptide template. An array of RAFT(c[-RGDfK-])n derivatives containing from one to sixteen clustered RGD motifs were synthesized and comparatively assayed in vitro on alphaVbeta3-expressing cells. Efficient inhibition of the alphaVbeta3-specific 23C6 monoclonal antibody fixation was observed with ligands displaying three and four copies of the cyclo[-RGDfK-] peptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • Humans
  • Integrin alphaVbeta3 / chemistry*
  • Integrins
  • Ligands
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry*
  • Peptides, Cyclic / chemical synthesis
  • Peptides, Cyclic / chemistry
  • Protein Binding

Substances

  • Integrin alphaVbeta3
  • Integrins
  • Ligands
  • Oligopeptides
  • Peptides, Cyclic
  • arginyl-glycyl-aspartic acid