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  • 1
    Electronic Resource
    Electronic Resource
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part B: Polymer Physics 36 (1998), S. 537-542 
    ISSN: 0887-6266
    Keywords: sulfonated polyelectrolytes ; gelatin ; complex stoichiometry ; size-exclusion chromatography ; flow field-flow fractionation ; hydrodynamic size ; Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: No abstract.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 40 (1998), S. 511-519 
    ISSN: 0021-9304
    Keywords: PEO chemistry ; cell adhesion ; model surface ; RGD peptide ; surface modification ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: The ability to study and regulate cell behavior at a biomaterial interface requires strict control over material surface chemistry. Perhaps the greatest challenge to researchers working in this area is preventing the fouling of a given surface due to uncontrolled protein adsorption. This work describes a method for coupling peptides to hydrophobic materials for the purpose of simultaneously preventing nonspecific protein adsorption and controlling cell adhesion. A hexapeptide containing the ubiquitous RGD cell-adhesion motif was coupled to polystyrene (PS) via a polyethylene oxide (PEO) tether in the form of a modified PEO/PPO/PEO triblock copolymer. Triblocks were adsorbed onto PS at a density of 3.3 ± (5.14 × 10-4) mg/m2 (1.4 × 105 ± 2.12 × 101 molecules/μm2), which was determined by isotope 125I labeling. The peptide, GRGDSY, was activated at the N terminus with N-Succinimidyl 3-(2-pyridyldithio) propionate and coupled to immobilized triblocks where the terminal hydroxyls had been converted to sulfhydryl groups. Surface peptide density was measured by amino acid analysis and found to be 1.4 × 104 ± 0.47 × 104 molecules/μm2. PS modified with PEO/PPO/PEO copolymers alone was found to be inert to cell adhesion both in the presence of serum proteins and when exposed to activated RGD peptide. In contrast, PS conjugated with RGD via end-group-activated PEO/PPO/PEO copolymers supported cell adhesion and spreading. The surface coupling scheme reported here should prove valuable for studying cell-ligand interactions under simplified and highly controlled conditions. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 40, 511-519, 1998.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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