Interrogating the Surface Interactions of Resilin-Like Peptides on h-BN and Graphene

Abstract

Resilin protein-based elastomers could provide pathways to synthetic materials with increased mechanical resilience; however, it remains challenging to replicate their properties when they are made in the lab. This is because Tyr-based cross-linking is necessary, which may require preorganized configurations of resilin in its natural environment. In previous work, the P1 graphene-binding peptide was conjugated with resilin-like peptides (RLPs) to produce P1/RLP conjugates. The binding of these peptides to the graphene surface was studied using QCM analysis and atomic force microscopy as an initial step toward preorganization for eventual cross-linking. Herein, the adsorption studies of RLPs (R1 and R2) and their conjugates with the P1 graphene-binding peptide are studied on hexagonal boron nitride (h-BN) using QCM analysis and molecular modeling. The results are compared with those of previous work based on the graphene surface. The binding affinity of P1/RLPs to h-BN is found to be similar to that of graphene, with notable changes that can be attributed to the variations in the surface composition. In addition, molecular simulations of the surface-adsorbed P1/RLP structures on h-BN indicate substantial differences compared to those on the graphene surface, with the RLP domain dominating the binding on h-BN. Moreover, the parent RLP peptides demonstrated increased binding to h-BN, which was not observed with graphene, thus indicating that h-BN is likely to be a poorer surface for peptide preorganization for eventual cross-linking for the controlled preparation of resilient elastomers.