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

Monique Aumailley, Marion Gurrath, Gerhard Müller, Juan Calvete, Rupert Timpl, Horst Kessler

Research output: Contribution to journalArticlepeer-review

541 Scopus citations

Abstract

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 or platelet receptor αIIbβ3 to fibrinogen. NMR studies of the two most active cyclic peptides showed for both an all-trans conformation with a βII′ and γ turn. Subtle conformational differences, however, exist between both peptides and may contribute to selectivity or inhibition.

Original languageEnglish
Pages (from-to)50-54
Number of pages5
JournalFEBS Letters
Volume291
Issue number1
DOIs
StatePublished - 7 Oct 1991

Keywords

  • Conformation
  • Fibrinogen receptor
  • Integrin
  • NMR
  • Synthetic peptide

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