Exploiting Materials\nBinding Peptides for the Organization\nof Resilient Biomolecular Constructs

Elastomers based on the resilin protein confer exceptional\nmechanical\nresilience in nature, but it remains elusive to recover the remarkable\nproperties of these materials when they are made in the laboratory.\nThis is possibly due to preorganized conformations of resilin in its\nnatural setting, facilitating Tyr-based cross-linking. Here, resilin-like\npeptides (RLPs) are conjugated with a graphene-binding peptide, P1,\nto produce P1/RLP conjugates, in which the P1 domain may provide favorable\npreorganization on a graphene surface. Experiments using quartz crystal\nmicrobalance analysis and atomic force microscopy identified that\nthe parent RLPs demonstrate negligible graphene binding; however,\nintegration of the P1 with the RLPs resulted in the formation of dense,\npatterned bioligand overlayers on graphene. To complement this, molecular\nsimulations revealed a notable difference in binding mode of the conjugates\ncompared with typical materials binding peptides. Specifically, the\nadsorption of the P1/RLP conjugates did not focus on a few strongly\nbound “anchor” residues, but instead supported a more\ndiffuse mode of binding, with many more participating residues featuring\nmoderate contact. Analysis of the number of available Tyr residues\n(i.e., those not adsorbed at the surface) indicate that the RLP2-based\nconjugates will provide greater opportunity for cross-linking when\nadsorbed on graphene, providing a framework to generate patterned\nelastomeric materials.