Arg-Gly-Asp constrained within cyclic pentapeptides. Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1

FEBS Lett. 1991 Oct 7;291(1):50-4. doi: 10.1016/0014-5793(91)81101-d.


Cyclic Arg-Gly-Asp-Phe-Val peptides with either D-Phe or D-Val residues were 20- to more than 100-fold better inhibitors of cell adhesion to vitronectin and/or laminin fragment P1 when compared to a linear variant or Gly-Arg-Gly-Asp-Ser. No or only little increase in inhibitory capacity was observed for fibronectin adhesion and for the binding of platelet receptor alpha IIb beta 3 to fibrinogen. NMR studies of the two most active cyclic peptides showed for both an all-trans conformation with a beta II' and gamma turn. Subtle conformational differences, however, exist between both peptides and may contribute to selectivity of inhibition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Adhesion*
  • Glycoproteins / metabolism*
  • Humans
  • Integrins / metabolism
  • Laminin / metabolism*
  • Mice
  • Molecular Sequence Data
  • Oligopeptides / chemistry*
  • Peptides, Cyclic / chemistry*
  • Protein Conformation
  • Structure-Activity Relationship
  • Vitronectin


  • Glycoproteins
  • Integrins
  • Laminin
  • Oligopeptides
  • Peptides, Cyclic
  • Vitronectin
  • arginyl-glycyl-aspartic acid