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Extracellular Matrix‐Like Surfactant Polymers Containing Arginine‐Glycine‐Aspartic Acid (RGD) Peptides
Author(s) -
Anderson Eric H.,
Ruegsegger Mark A.,
Murugesan Gurunathan,
KottkeMarchant Kandice,
Marchant Roger E.
Publication year - 2004
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200300125
Subject(s) - chemistry , peptide , pulmonary surfactant , polymer , polymer chemistry , dextran , aspartic acid , vinyl alcohol , biophysics , amino acid , organic chemistry , biochemistry , biology
Summary: 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‐GSSSG RGD SPA‐NH 2 (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.