Discovery of a sulfated tetrapeptide that binds to vascular endothelial growth factor

Heather D. Maynard, Jeffrey A. Hubbell

Research output: Contribution to journalArticlepeer-review

66 Scopus citations


Molecules that mimic the sulfated glycosaminoglycan heparin and bind to heparin-binding growth factors would serve as important building blocks for synthetic biomaterials, e.g. to create a growth factor reservoir within a matrix. Peptide-based heparin mimetics would be particularly attractive, given the ease of peptide synthesis and modification. A sulfated tetrapeptide that fits this description and binds to vascular endothelial growth factor (VEGF) was discovered using a rationally-designed combinatorial approach. A ∼6600 member library of tetrapeptides, designed to include heparin functionality, was synthesized by solid-phase Fmoc chemistry. The library was analyzed on-resin for VEGF binding using a fluorescence assay that employed a 7-amino-4-methylcoumarin-modified VEGF165. The beads were ranked according to fluorescent signal and SY(SO3) DY(SO3) was identified as the top binder. The binding affinity of the peptide for VEGF165 was ascertained by surface plasmon resonance and compared with the heparin mimic suramin; the peptide binds to VEGF165 100-fold stronger than the sulfonated compound. These results suggest that the identified peptide may be useful in biomaterial applications where binding of VEGF is desired.

Original languageEnglish (US)
Pages (from-to)451-459
Number of pages9
JournalActa Biomaterialia
Issue number4
StatePublished - Jul 2005
Externally publishedYes


  • Heparin mimic
  • Library
  • Sulfated peptide
  • VEGF

ASJC Scopus subject areas

  • Biomaterials
  • Biomedical Engineering
  • Biotechnology
  • Biochemistry
  • Molecular Biology


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