Peptide amphiphile nanostructure-heparin interactions and their relationship to bioactivity

Kanya Rajangam, Michael S. Arnold, Mark A. Rocco, Samuel I Stupp

Research output: Contribution to journalArticle

92 Citations (Scopus)

Abstract

Heparin-protein interactions are important in many physiological processes including angiogenesis, the growth of new blood vessels from existing ones. We have previously developed a highly angiogenic self-assembling gel, wherein the self-assembly process is triggered by the interactions between heparin and peptide amphiphiles (PAs) with a consensus heparin binding sequence. In this report, this consensus sequence was scrambled and incorporated into a new peptide amphiphile in order to study its importance in heparin interaction and bioactivity. Heparin was able to trigger gel formation of the scrambled peptide amphiphile (SPA). Furthermore, the affinity of the scrambled molecule for heparin was unchanged as shown by isothermal titration calorimetry and high Förster resonance emission transfer efficiency. However, both the mobile fraction and the dissociation rate constant of heparin, using fluorescence recovery after photobleaching, were markedly higher in its interaction with the scrambled molecule implying a weaker association. Importantly, the scrambled peptide amphiphile-heparin gel had significantly less angiogenic bioactivity as shown by decreased tubule formation of sandwiched endothelial cells. Hence, we believe that the presence of the consensus sequence stabilizes the interaction with heparin and is important for the bioactivity of these new materials.

Original languageEnglish
Pages (from-to)3298-3305
Number of pages8
JournalBiomaterials
Volume29
Issue number23
DOIs
Publication statusPublished - Aug 2008

Fingerprint

Amphiphiles
Nanostructures
Bioactivity
Peptides
Heparin
Gels
Consensus Sequence
Physiological Phenomena
Fluorescence Recovery After Photobleaching
Photobleaching
Calorimetry
Molecules
Endothelial cells
Blood vessels
Titration
Self assembly
Blood Vessels
Rate constants
Endothelial Cells
Fluorescence

Keywords

  • Angiogenesis
  • Heparin
  • Nanoparticle
  • Self-assembly

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering

Cite this

Peptide amphiphile nanostructure-heparin interactions and their relationship to bioactivity. / Rajangam, Kanya; Arnold, Michael S.; Rocco, Mark A.; Stupp, Samuel I.

In: Biomaterials, Vol. 29, No. 23, 08.2008, p. 3298-3305.

Research output: Contribution to journalArticle

Rajangam, Kanya ; Arnold, Michael S. ; Rocco, Mark A. ; Stupp, Samuel I. / Peptide amphiphile nanostructure-heparin interactions and their relationship to bioactivity. In: Biomaterials. 2008 ; Vol. 29, No. 23. pp. 3298-3305.
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