title: Nanoscale clustering of RGD peptides at surfaces using Comb polymers. 1. Synthesis and characterization of Comb thin films.
abstract: Theoretical and experimental studies were conducted to elucidate the structure and properties of amphiphilic comb polymer thin films presenting nanoscale clusters of Arg-Gly-Asp (RGD) peptides for control of cell adhesion on biomaterials. Combs comprised of a poly(methyl methacrylate) backbone and short poly(ethylene oxide) side chains were synthesized, and peptides were tethered to the side chain ends to create nanoscale peptide clusters. In thin films, comb polymers containing >or = 30 wt % six to nine unit PEO side chains completely resisted adhesion of a model fibroblast cell line in the presence of 7.5% serum over 24 h. These same polymers modified with RGD peptides elicited tunable cell adhesion when mixed with unmodified combs in varying proportion. A self-consistent field lattice model of the interface between comb polymer films and water predicts an organization of the top molecular layer of comb polymer with the backbone oriented parallel to the interface in quasi-two-dimensional confinement and hydrophilic side chains extended in a brushlike layer into solution. This picture of a quasi-2D configuration is consistent with the observed surface properties of comb films in water as well as measurements of the RGD cluster density on mixed comb surfaces using fluorescent nanosphere labeling of ligand clusters.
authors.affiliation: Department of Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
authors.forename: D J
authors.initials: DJ
authors.lastname: Irvine
authors.forename: A M
authors.initials: AM
authors.lastname: Mayes
authors.forename: L G
authors.initials: LG
authors.lastname: Griffith
mesh_terms: D002448:Cell Adhesion; D005109:Extracellular Matrix / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008832:Microchemistry; D008863:Microspheres; D008954:Models, Biological; D015394:Molecular Structure; D036103:Nanotechnology; D009842:Oligopeptides / Q000737:chemistry*; D011108:Polymers / Q000138:chemical synthesis* / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D009842:Oligopeptides; D011108:Polymers; C047981:arginyl-glycyl-aspartic acid