Synthesis and Cell Adhesive Properties of Linear and Cyclic RGD Functionalized Polynorbornene Thin Films
Autor: | Ying Y. Lu, Eileen Fong, Wilson C. Ho, Paresma R. Patel, David A. Tirrell, Robert H. Grubbs, Rosemary Conrad Kiser |
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Přispěvatelé: | School of Materials Science & Engineering |
Jazyk: | angličtina |
Rok vydání: | 2012 |
Předmět: |
Polymers and Plastics
Cell Survival Biocompatible Materials Bioengineering Peptide Polyethylene glycol Article Polyethylene Glycols Polymerization Biomaterials chemistry.chemical_compound Polymer chemistry Cell Adhesion Human Umbilical Vein Endothelial Cells Materials Chemistry Humans Cell adhesion Cells Cultured Integrin binding chemistry.chemical_classification Tissue Engineering Hydrogels ROMP Adhesion Monomer chemistry Self-healing hydrogels Oligopeptides Plastics Protein Binding |
Popis: | Described herein is the efficient synthesis and evaluation of bioactive arginine-glycine-aspartic acid (RGD) functionalized polynorbornene-based materials for cell adhesion and spreading. Polynorbornenes containing either linear or cyclic RGD peptides were synthesized by ring-opening metathesis polymerization (ROMP) using the well-defined ruthenium initiator [(H_(2)IMes)(pyr)_(2)(Cl)_(2)Ru═CHPh]. The random copolymerization of three separate norbornene monomers allowed for the incorporation of water-soluble polyethylene glycol (PEG) moieties, RGD cell recognition motifs, and primary amines for postpolymerization cross-linking. Following polymer synthesis, thin-film hydrogels were formed by cross-linking with bis(sulfosuccinimidyl) suberate (BS^3), and the ability of these materials to support human umbilical vein endothelial cell (HUVEC) adhesion and spreading was evaluated and quantified. When compared to control polymers containing either no peptide or a scrambled RDG peptide, polymers with linear or cyclic RGD at varying concentrations displayed excellent cell adhesive properties in both serum-supplemented and serum-free media. Polymers with cyclic RGD side chains maintained cell adhesion and exhibited comparable integrin binding at a 100-fold lower concentration than those carrying linear RGD peptides. The precise control of monomer incorporation enabled by ROMP allows for quantification of the impact of RGD structure and concentration on cell adhesion and spreading. The results presented here will serve to guide future efforts for the design of RGD functionalized materials with applications in surgery, tissue engineering, and regenerative medicine. |
Databáze: | OpenAIRE |
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