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Sequence–Structure–Property Relationships of Recombinant Spider Silk Proteins: Integration of Biopolymer Design, Processing, and Modeling

Authors

  • Sreevidhya Tarakkad Krishnaji,

    1. Departments of Chemistry & Biomedical Engineering, Tufts University, Medford, MA 02155, USA
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  • Graham Bratzel,

    1. Laboratory for Atomistic and Molecular Mechanics, Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
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  • Michelle E. Kinahan,

    1. Department of Biomedical Engineering, Boston University, Boston, MA 02215, USA
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  • Jonathan A. Kluge,

    1. Departments of Chemistry & Biomedical Engineering, Tufts University, Medford, MA 02155, USA
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  • Cristian Staii,

    1. Department of Physics & Astronomy, Tufts University, Medford, MA 02155, USA
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  • Joyce Y. Wong,

    Corresponding author
    1. Department of Biomedical Engineering, Boston University, Boston, MA 02215, USA
    • Department of Biomedical Engineering, Boston University, Boston, MA 02215, USA
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  • Markus J. Buehler,

    Corresponding author
    1. Laboratory for Atomistic and Molecular Mechanics, Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
    • Laboratory for Atomistic and Molecular Mechanics, Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
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  • David L. Kaplan

    Corresponding author
    1. Departments of Chemistry & Biomedical Engineering, Tufts University, Medford, MA 02155, USA
    • Departments of Chemistry & Biomedical Engineering, Tufts University, Medford, MA 02155, USA.
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Abstract

The mechanical properties of spider silks drive interest as sources of new materials. However, there remains a lot to learn regarding the relationships between sequence, structure, and mechanical properties. In order to predict the types of sequence–functional relationships, synthesis–characterization–computation are integrated using recombinant spider silk-like block copolymers. Two designs are studied, both with origins from the spider Nephila clavipes. These proteins are studied both experimentally and in silico to understand the relationships between sequence chemistry, processing, structure, and materials function. Films formed from the two proteins are thoroughly characterized. In parallel, molecular modeling is used to assess the propensity of the two sequences to form β-sheets or crystalline structures. The results demonstrate that the modeling predicts the structural differences between the two silk-like polymers and these features can also be related to differences in functional outcomes. With this example of relating sequence design (hydrophobic–hydrophilic domains), experiment (genetic design and synthesis), processing (film and fiber formation) and modeling (predictions of crystallinity), synergy among these methods is demonstrated for predictable material outcomes. This approach offers a robust discovery path when looking towards next generation approaches to targeted materials outcomes.

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