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Complete recombinant silk-elastinlike protein-based tissue scaffold.


ABSTRACT: Due to their improved biocompatibility and specificity over synthetic materials, protein-based biomaterials, either derived from natural sources or genetically engineered, have been widely fabricated into nanofibrous scaffolds for tissue engineering applications. However, their inferior mechanical properties often require the reinforcement of protein-based tissue scaffolds using synthetic polymers. In this study, we report the electrospinning of a completely recombinant silk-elastinlike protein-based tissue scaffold with excellent mechanical properties and biocompatibility. In particular, SELP-47K containing tandemly repeated polypeptide sequences derived from native silk and elastin was electrospun into nanofibrous scaffolds, and stabilized via chemical vapor treatment and mechanical preconditioning. When fully hydrated in 1× PBS at 37 °C, mechanically preconditioned SELP-47K scaffolds displayed elastic moduli of 3.4-13.2 MPa, ultimate tensile strengths of 5.7-13.5 MPa, deformabilities of 100-130% strain, and resilience of 80.6-86.9%, closely matching or exceeding those of protein-synthetic blend polymeric scaffolds. Additionally, SELP-47K nanofibrous scaffolds promoted cell attachment and growth, demonstrating their in vitro biocompatibility.

SUBMITTER: Qiu W 

PROVIDER: S-EPMC3006068 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

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Complete recombinant silk-elastinlike protein-based tissue scaffold.

Qiu Weiguo W   Huang Yiding Y   Teng Weibing W   Cohn Celine M CM   Cappello Joseph J   Wu Xiaoyi X  

Biomacromolecules 20101108 12


Due to their improved biocompatibility and specificity over synthetic materials, protein-based biomaterials, either derived from natural sources or genetically engineered, have been widely fabricated into nanofibrous scaffolds for tissue engineering applications. However, their inferior mechanical properties often require the reinforcement of protein-based tissue scaffolds using synthetic polymers. In this study, we report the electrospinning of a completely recombinant silk-elastinlike protein-  ...[more]

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