Inhibition of cell adhesion to fibronectin by oligopeptide-substituted polynorbornenes
| Autor: | Heather D. Maynard, Sheldon Y. Okada, Robert H. Grubbs |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Magnetic Resonance Spectroscopy
Stereochemistry Polymers Integrin Peptide Biochemistry Catalysis Cell Line Colloid and Surface Chemistry Polymer chemistry Cell Adhesion Humans Cell adhesion chemistry.chemical_classification Oligopeptide biology Chemistry Biological activity General Chemistry ROMP Fibroblasts Ligand (biochemistry) Fibronectins Fibronectin Models Chemical biology.protein Oligopeptides Plastics |
| Zdroj: | Journal of the American Chemical Society. 123(7) |
| ISSN: | 0002-7863 |
| Popis: | Polynorbornenes substituted with two different peptide sequences from the RGD-containing integrin cell-binding domain of fibronectin are potent inhibitors of human foreskin fibroblast cell adhesion to fibronectin-coated surfaces. Ring-opening metathesis polymerization (ROMP) using Ru==CHPh(Cl)(2)(PCy(3))(DHIMes) (1) as an initiator produced polymers substituted with GRGDS and PHSRN peptide sequences. The inhibitory activity was quantified for these polymers and compared to the free peptides and GRGES-containing controls. A homopolymer substituted with GRGDS peptides was significantly more active than the free GRGDS peptide (IC(50) of 0.18 +/- 0.03 and 1.33 +/- 0.20 mM respectively), and the copolymer containing both GRGDS and PHSRN is the most potent inhibitor (IC(50) of 0.04 +/- 0.01 mM). These results demonstrate that significant enhancements of observed biological activity can be obtained from polymeric materials containing more than one type of multivalent ligand and that ROMP is a useful method to synthesize such well-defined copolymers. |
| Databáze: | OpenAIRE |
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