title: Construction of multifunctional proteins for tissue engineering: epidermal growth factor with collagen binding and cell adhesive activities.
abstract: The development of different techniques based on natural and polymeric scaffolds are useful for the design of different biomimetic materials. These approaches, however, require supplementary steps for the chemical or physical modification of the biomaterial. To avoid such steps, in the present study, we constructed a new multifunctional protein that can be easily immobilized onto hydrophobic surfaces, and at the same time helps enhance specific cell adhesion and proliferation onto collagen substrates. A collagen binding domain was fused to a previously constructed protein, which had an epidermal growth factor fused to a hydrophobic peptide that allows for cell adhesion. The new fusion protein, designated fnCBD-ERE-EGF is produced in Escherichia coli, and its abilities to bind to collagen and promote cell proliferation were investigated. fnCBD-ERE-EGF was shown to keep both collagen binding and cell growth-promoting activities comparable to those of the corresponding unfused proteins. The results obtained in this study also suggest the use of a fnCBD-ERE-EGF as an alternative for the design of multifunctional ECM-bound growth factor based materials.
authors.affiliation: Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
authors.forename: Elloumi
authors.initials: E
authors.lastname: Hannachi Imen
authors.forename: Makiko
authors.initials: M
authors.lastname: Nakamura
authors.forename: Masayasu
authors.initials: M
authors.lastname: Mie
authors.forename: Eiry
authors.initials: E
authors.lastname: Kobatake
mesh_terms: D040761:Biomimetic Materials / Q000378:metabolism; D002448:Cell Adhesion; D002460:Cell Line; D049109:Cell Proliferation; D003094:Collagen / Q000378:metabolism*; D004549:Elastin / Q000235:genetics / Q000378:metabolism; D004815:Epidermal Growth Factor / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D055767:Immobilized Proteins / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D009842:Oligopeptides / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D023822:Tissue Engineering
chemical_list: D055767:Immobilized Proteins; D009842:Oligopeptides; D011993:Recombinant Fusion Proteins; D004815:Epidermal Growth Factor; C047981:arginyl-glycyl-aspartic acid; D003094:Collagen; D004549:Elastin