Organization of Resilin-like Peptides in Three Dimensions Using Au Nanoparticles

Nature provides a palette of materials with properties ranging from strong and tough to flexible and elastomeric. Resilin, a protein in insects, can generate resilient elastomers cross-linked at tyrosine residues. These elastomers rival or exceed the properties of synthetic materials, making it desirable to mimic the natural system. Herein, we demonstrate the use of biomolecules that incorporate resilin-like peptides (RLPs), identified from resilin, with Au binding domains. These sequences bind Au interfaces to preorganize RLPs for eventual cross-linking. This approach could be exploited to generate elastomers that mimic the Au structure. Through this analysis, sequence effects were identified that could optimize peptide domain ordering on Au to controllably cross-link the biomolecules, leading to elastomer formation. Furthermore, nanoparticle synthesis studies indicated that Au binding domain inclusion was critical to generate monodisperse materials (in both shape and size). Such results provide pathways for controllable peptide cross-linking on surfaces for biostructural formation.