Peptide ligands for integrin alpha v beta 3 selected from random phage display libraries

Biochemistry. 1995 Mar 28;34(12):3948-55. doi: 10.1021/bi00012a012.


The integrin alpha v beta 3 binds promiscuously to cell-adhesive proteins: vitronectin, fibronectin, and several others containing the RGD motif. We have explored molecular recognition by alpha v beta 3 through selection of ligands from large random libraries of peptides displayed on phage. Ligands bound by alpha beta 3 consisted primarily of RGD peptides; however, these peptides showed considerable heterogeneity with respect to the identities of amino acids flanking RGD. The tolerance of alpha v beta 3 for RGD peptides of diverse composition is consistent with its role in vivo as a versatile receptor for RGD-containing extracellular matrix proteins. Peptide ligands for alpha v beta 3 also included a novel binding sequence, identical to a tetrapeptide found in vitronectin, which is a candidate for a synergistic site in this adhesive protein that may act in concert with RGD to promote molecular recognition.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Bacteriophages
  • Base Sequence
  • DNA Primers
  • Extracellular Matrix Proteins / metabolism*
  • Female
  • Humans
  • Integrins / isolation & purification
  • Integrins / metabolism*
  • Molecular Sequence Data
  • Oligopeptides / metabolism*
  • Placenta / metabolism
  • Pregnancy
  • Protein Binding
  • Random Allocation
  • Receptors, Cytoadhesin / isolation & purification
  • Receptors, Cytoadhesin / metabolism*
  • Receptors, Vitronectin
  • Structure-Activity Relationship
  • Templates, Genetic


  • DNA Primers
  • Extracellular Matrix Proteins
  • Integrins
  • Oligopeptides
  • Receptors, Cytoadhesin
  • Receptors, Vitronectin
  • arginyl-glycyl-aspartic acid