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    Structure-Property Relationship Based on the Amino Acid Composition of Recombinant Spider Silk Proteins for Potential Biomedical Applications

    Year: 2022

    Journal: ACS Appl. Mater. Interfaces, Volume 14, JUL 20, page 31751–31766

    Authors: Lentz, Sarah; Trossmann, Vanessa T.; Borkner, Christian B.; Beyersdorfer, Vivien; Rottmar, Markus; Scheibel, Thomas

    Organizations: Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [326998133-TRR225, DFG SCHE603/23-1]

    Keywords: recombinant spider silk proteins; blood coagulation; enzymatic degradation; cell adhesion; protein adsorption; surface properties

    ABSTRACT: Improving biomaterials by engineering applicationspecific and adjustable properties is of increasing interest. Most of the commonly available materials fulfill the mechanical and physical requirements of relevant biomedical applications, but they lack biological functionality, including biocompatibility and prevention of microbial infestation. Thus, research has focused on customizable, application-specific, and modifiable surface coatings to cope with the limitations of existing biomaterials. In the case of adjustable degradation and configurable interaction with body fluids and cells, these coatings enlarge the applicability of the underlying biomaterials. Silks are interesting coating materials, e.g., for implants, since they exhibit excellent biocompatibility and mechanical properties. Herein, we present putative implant coatings made of five engineered recombinant spider silk proteins derived from the European garden spider Araneus diadematus fibroins (ADF), differing in amino acid sequence and charge. We analyzed the influence of the underlying amino acid composition on wetting behavior, blood compatibility, biodegradability, serum protein adsorption, and cell adhesion. The outcome of the comparison indicates that spider silk coatings can be engineered for explicit biomedical applications.
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