title: Electrospun silk-elastin-like fibre mats for tissue engineering applications.
abstract: Protein-based polymers are present in a wide variety of organisms fulfilling structural and mechanical roles. Advances in protein engineering and recombinant DNA technology allow the design and production of recombinant protein-based polymers (rPBPs) with an absolute control of its composition. Although the application of recombinant proteins as biomaterials is still an emerging technology, the possibilities are limitless and far superior to natural or synthetic materials, as the complexity of the structural design can be fully customized. In this work, we report the electrospinning of two new genetically engineered silk-elastin-like proteins (SELPs) consisting of alternate silk- and elastin-like blocks. Electrospinning was performed with formic acid and aqueous solutions at different concentrations without addition of further agents. The size and morphology of the electrospun structures was characterized by scanning electron microscopy showing its dependence on the concentration and solvent used. Treatment with methanol-saturated air was employed to stabilize the structure and promote water insolubility through a time-dependent conversion of random coils into β-sheets (FTIR). The resultant methanol-treated electrospun mats were characterized for swelling degree (570-720%), water vapour transmission rate (1083 g/m(2)/day) and mechanical properties (modulus of elasticity ∼126 MPa). Furthermore, the methanol-treated SELP fibre mats showed no cytotoxicity and were able to support adhesion and proliferation of normal human skin fibroblasts. Adhesion was characterized by a filopodia-mediated mechanism. These results demonstrate that SELP fibre mats can provide promising solutions for the development of novel biomaterials suitable for tissue engineering applications.
authors.affiliation: CBMA (Centre of Molecular and Environmental Biology), Department of Biology, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal.
authors.forename: Raul
authors.initials: R
authors.lastname: Machado
authors.forename: André
authors.initials: A
authors.lastname: da Costa
authors.forename: Vitor
authors.initials: V
authors.lastname: Sencadas
authors.forename: Carmen
authors.initials: C
authors.lastname: Garcia-Arévalo
authors.forename: Carlos M
authors.initials: CM
authors.lastname: Costa
authors.forename: Jorge
authors.initials: J
authors.lastname: Padrão
authors.forename: Andreia
authors.initials: A
authors.lastname: Gomes
authors.forename: Senentxu
authors.initials: S
authors.lastname: Lanceros-Méndez
authors.forename: José Carlos
authors.initials: JC
authors.lastname: Rodríguez-Cabello
authors.forename: Margarida
authors.initials: M
authors.lastname: Casal
mesh_terms: D001672:Biocompatible Materials / Q000737:chemistry; D001696:Biomechanical Phenomena; D002448:Cell Adhesion; D002460:Cell Line; D049109:Cell Proliferation; D002470:Cell Survival; D004549:Elastin / Q000737:chemistry* / Q000235:genetics; D005347:Fibroblasts / Q000166:cytology; D006801:Humans; D008422:Materials Testing; D008855:Microscopy, Electron, Scanning; D015202:Protein Engineering; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D047011:Silk / Q000737:chemistry* / Q000235:genetics; D023822:Tissue Engineering / Q000379:methods*; D054457:Tissue Scaffolds / Q000737:chemistry
chemical_list: D001672:Biocompatible Materials; D011993:Recombinant Fusion Proteins; D047011:Silk; D004549:Elastin