[ { "id": "authors:gs9p1-v4283", "collection": "authors", "collection_id": "gs9p1-v4283", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20120926-114920502", "type": "article", "title": "Synthesis and Cell Adhesive Properties of Linear and Cyclic RGD Functionalized Polynorbornene Thin Films", "author": [ { "family_name": "Patel", "given_name": "Paresma R.", "clpid": "Patel-P-R" }, { "family_name": "Kiser", "given_name": "Rosemary Conrad", "clpid": "Kiser-R-C" }, { "family_name": "Lu", "given_name": "Ying Y.", "clpid": "Lu-Ying-Yu" }, { "family_name": "Fong", "given_name": "Eileen", "clpid": "Fong-Eileen" }, { "family_name": "Ho", "given_name": "Wilson C.", "clpid": "Ho-Wilson-C" }, { "family_name": "Tirrell", "given_name": "David A.", "orcid": "0000-0003-3175-4596", "clpid": "Tirrell-D-A" }, { "family_name": "Grubbs", "given_name": "Robert H.", "orcid": "0000-0002-0057-7817", "clpid": "Grubbs-R-H" } ], "abstract": "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\u2550CHPh]. 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.", "doi": "10.1021/bm300795y", "pmcid": "PMC3442365", "issn": "1525-7797", "publisher": "American Chemical Society", "publication": "Biomacromolecules", "publication_date": "2012-08", "series_number": "8", "volume": "13", "issue": "8", "pages": "2546-2553" }, { "id": "authors:642yj-tyt61", "collection": "authors", "collection_id": "642yj-tyt61", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20110202-085127824", "type": "article", "title": "Collective Cell Migration on Artificial Extracellular Matrix Proteins Containing Full-Length Fibronectin Domains", "author": [ { "family_name": "Fong", "given_name": "Eileen", "clpid": "Fong-Eileen" }, { "family_name": "Tirrell", "given_name": "David A.", "orcid": "0000-0003-3175-4596", "clpid": "Tirrell-D-A" } ], "abstract": "Protein-based biomaterials that promote rapid wound healing are prepared by expression of artificial genes in bacterial cells. Artificial extracellular matrix proteins containing full-length fibronectin domains 9 and 10 exhibit strong \u03b1_5\u03b2_1 integrin binding and support rapid spreading, proliferation, and collective migration of fibroblasts.", "doi": "10.1002/adma.201002448", "pmcid": "PMC3027490", "issn": "0935-9648", "publisher": "Wiley", "publication": "Advanced Materials", "publication_date": "2010-12-07", "series_number": "46", "volume": "22", "issue": "46", "pages": "5271-5275" }, { "id": "authors:t6008-pbb21", "collection": "authors", "collection_id": "t6008-pbb21", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20101206-122849107", "type": "article", "title": "Boundary crossing in epithelial wound healing", "author": [ { "family_name": "Fong", "given_name": "Eileen", "clpid": "Fong-Eileen" }, { "family_name": "Tzlil", "given_name": "Shelly", "clpid": "Tzlil-Shelly" }, { "family_name": "Tirrell", "given_name": "David A.", "orcid": "0000-0003-3175-4596", "clpid": "Tirrell-D-A" } ], "abstract": "The processes of wound healing and collective cell migration have been studied for decades. Intensive research has been devoted to understanding the mechanisms involved in wound healing, but the role of cell-substrate interactions is still not thoroughly understood. Here we probe the role of cell-substrate interactions by examining in vitro the healing of monolayers of human corneal epithelial (HCE) cells cultured on artificial extracellular matrix (aECM) proteins. We find that the rate of wound healing is dependent on the concentration of fibronectin-derived (RGD) cell-adhesion ligands in the aECM substrate. The wound closure rate varies nearly sixfold on the substrates examined, despite the fact that the rates of migration and proliferation of individual cells show little sensitivity to the RGD concentration (which varies 40-fold). To explain this apparent contradiction, we study collective migration by means of a dynamic Monte Carlo simulation. The cells in the simulation spread, retract, and proliferate with probabilities obtained from a simple phenomenological model. The results indicate that the overall wound closure rate is determined primarily by the rate at which cells cross the boundary between the aECM protein and the matrix deposited under the cell sheet.", "doi": "10.1073/pnas.1008291107", "pmcid": "PMC2984212", "issn": "0027-8424", "publisher": "National Academy of Sciences", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "publication_date": "2010-11-09", "series_number": "45", "volume": "107", "issue": "45", "pages": "19302-19307" } ]