A supramolecular platform stabilizing growth factors

Simone I.S. Hendrikse, Sergio Spaans, E.W. Meijer, Patricia Y.W. Dankers

Research output: Contribution to journalArticleAcademicpeer-review

11 Citations (Scopus)
113 Downloads (Pure)


High concentrations of supplemented growth factors can cause oversaturation and adverse effects in in vitro and in vivo studies. Though, these supraphysiological concentrations are often required due to the low stability of growth factors. Here we demonstrate the stabilization of TGF-β1 and BMP4 using supramolecular polymers. Inspired by heparan sulfate, sulfonated peptides were presented on a supramolecular polymer to allow for non-covalent binding to growth factors in solution. After mixing with excipient molecules, both TGF-β1 and BMP4 were shown to have a prolonged half-life compared to the growth factors free in solution. Moreover, high cellular response was measured by a luciferase assay, indicating that TGF-β1 remained highly active upon binding to the supramolecular assembly. The results demonstrate that significant lower concentrations of growth factors can be used when supramolecular polymers bearing growth factor binding moieties are implemented. This approach can also be exploited in hydrogel systems to control growth factor release.

Original languageEnglish
Pages (from-to)2610-2617
Number of pages8
Issue number7
Publication statusPublished - 9 Jul 2018


  • Bone Morphogenetic Protein 4/chemistry
  • Cell Line, Tumor
  • Humans
  • Polymers/chemistry
  • Protein Binding
  • Protein Stability
  • Pyrimidinones/chemistry
  • Transforming Growth Factor beta/chemistry


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