The Platelet Integrin αIIbβ3 Binds to the RGD and AGD Motifs in Fibrinogen

Juan Sánchez-Cortés, Milan Mrksich*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

35 Scopus citations


Fibrinogen (Fbg) mediates platelet aggregation by binding the αIIbβ3 integrin receptor, but the interaction of the receptor with peptide motifs of Fbg remains unresolved. This paper describes the use of self-assembled monolayers (SAMs) to study the adhesion of αIIbβ3-transfected CHO cells to the GRGDS and HHLGGAKQAGDV motifs within Fbg. Cells adhered to and spread on monolayers presenting either peptide. Cell adhesion could be inhibited by either soluble peptide, demonstrating that the peptides bind competitively to the integrin. A peptide array was used to show that AGD was the minimal binding sequence in HHLGGAKQAGDV and that the receptor recognizes ligands of the form GXGDSC, where X is a hydrophobic or basic residue. This work revises our understanding of the αIIbβ3 specificity and also suggests a new class of antithrombotic agents.

Original languageEnglish (US)
Pages (from-to)990-1000
Number of pages11
JournalChemistry and Biology
Issue number9
StatePublished - Sep 25 2009



ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry

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