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1.
Biomaterials ; 30(3): 277-86, 2009 Jan.
Article in English | MEDLINE | ID: mdl-18929406

ABSTRACT

Biomaterials used in implants have traditionally been selected based on their mechanical properties, chemical stability, and biocompatibility. However, the durability and clinical efficacy of implantable biomedical devices remain limited in part due to the absence of appropriate biological interactions at the implant interface and the lack of integration into adjacent tissues. Herein, we describe a robust peptide-based coating technology capable of modifying the surface of existing biomaterials and medical devices through the non-covalent binding of modular biofunctional peptides. These peptides contain at least one material binding sequence and at least one biologically active sequence and thus are termed, "Interfacial Biomaterials" (IFBMs). IFBMs can simultaneously bind the biomaterial surface while endowing it with desired biological functionalities at the interface between the material and biological realms. We demonstrate the capabilities of model IFBMs to convert native polystyrene, a bioinert surface, into a bioactive surface that can support a range of cell activities. We further distinguish between simple cell attachment with insufficient integrin interactions, which in some cases can adversely impact downstream biology, versus biologically appropriate adhesion, cell spreading, and cell survival mediated by IFBMs. Moreover, we show that we can use the coating technology to create spatially resolved patterns of fluorophores and cells on substrates and that these patterns retain their borders in culture.


Subject(s)
Biocompatible Materials/metabolism , Materials Testing , Peptides/metabolism , Polystyrenes/metabolism , Amino Acid Sequence , Apoptosis , Biotin/metabolism , Cell Adhesion , Cell Movement , Cell Proliferation , Cell Survival , Cells, Cultured , Coated Materials, Biocompatible , Endothelial Cells/cytology , Endothelial Cells/metabolism , Fluorescein-5-isothiocyanate/metabolism , Humans , Microscopy, Atomic Force , Molecular Sequence Data , Peptides/chemistry , Surface Properties
2.
Chem Biol ; 13(7): 695-700, 2006 Jul.
Article in English | MEDLINE | ID: mdl-16873017

ABSTRACT

Amphiphilic macromolecules containing a polystyrene-adherent peptide domain and a cell-repellent poly(ethylene glycol) domain were designed, synthesized, and evaluated as a cytophobic surface coating. Such cytophobic, or cell-repellent, coatings are of interest for varied medical and biotechnological applications. The composition of the polystyrene binding peptide domain was identified using an M13 phage display library. ELISA and atomic force spectroscopy were used to evaluate the binding affinity of the amphiphile peptide domain to polystyrene. When coated onto polystyrene, the amphiphile reduced cell adhesion of two distinct mammalian cell lines and pathogenic Staphylococcus aureus strains.


Subject(s)
Peptides/chemistry , Polyethylene Glycols/chemistry , Amino Acid Sequence , Bacterial Adhesion , Enzyme-Linked Immunosorbent Assay , Humans , Microscopy, Atomic Force , Molecular Sequence Data , Staphylococcus aureus/physiology
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