Extracellular Matrix-Like Surfactant Polymers Containing Arginine-Glycine-Aspartic Acid (RGD) Peptides

We report on a novel series of biomimetic polymers exhibiting interfacial properties similar to the extracellular matrix. A series of well‐defined surfactant polymers were synthesized by simultaneously incorporating arginine‐glycine‐aspartic acid (RGD) peptide, dextran oligosaccharide, and hexyl lig...

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Veröffentlicht in:Macromolecular bioscience 2004-08, Vol.4 (8), p.766-775
Hauptverfasser: Anderson, Eric H., Ruegsegger, Mark A., Murugesan, Gurunathan, Kottke-Marchant, Kandice, Marchant, Roger E.
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Sprache:eng
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Zusammenfassung:We report on a novel series of biomimetic polymers exhibiting interfacial properties similar to the extracellular matrix. A series of well‐defined surfactant polymers were synthesized by simultaneously incorporating arginine‐glycine‐aspartic acid (RGD) peptide, dextran oligosaccharide, and hexyl ligands with controlled feed ratios onto a poly(vinyl amine) (PVAm) backbone. The peptide sequence was H‐GSSSGRGDSPA‐NH2 (Pep) having a hydrophilic extender at the amino terminus and capped carboxy terminus. The peptide‐to‐dextran (Pep:Dex) ratios were varied to create surfactants having 0, 25, 50, 75, and 100 mol‐% peptide relative to dextran. The surfactants were characterized by IR, NMR and atomic force microscopy (AFM) for composition and surface active properties. AFM confirmed full surface coverage of PVAm(Pep)(100%) on graphite, and supported the mechanism of interdigitation of hexyl ligands between surfactant molecules within a specified range of hexyl chain densities. the attachment and growth of human pulmonary artery endothelial cells on the PVAm(Pep)(100%) surface was identical to the fibronectin positive control. Cell adhesion decreased dramatically with decreasing peptide density on the surfactant polymers. Molecular model of a peptide surfactant polymer, consisting of poly(vinyl amine) backbone with peptide, dextran oligosaccharide and hexyl branches coupled to the polymer chain.
ISSN:1616-5187
1616-5195
DOI:10.1002/mabi.200300125