Aqueous Graphene Dispersion and Biofunctionalization via Enzymatic Oxidation of Tripeptides.

Graphene, a 2D carbon material, possesses extraordinary mechanical, electrical, and thermal properties, making it highly attractive for various biological applications such as biosensing, biotherapeutics, and tissue engineering. However, the tendency of graphene sheets to aggregate and restack hinders its dispersion in water, limiting these applications. Peptides, with their defined amino acid sequences and versatile functionalities, are compelling molecules with which to modify graphene-aromatic amino acids can strengthen interactions through π-stacking and charged groups can be chosen to make the sheets dispersible and stable in water. Here, a facile and green method for covalently functionalizing and dispersing graphene using amphiphilic tripeptides, facilitated by a tyrosine phenol side chain, through an aqueous enzymatic oxidation process is demonstrated. The presence of a second aromatic side chain group enhances this interaction through non-covalent support via π-π stacking with the graphene surface. Futhermore, the addition of charged moieties originating from either ionizable amino acids or terminal groups facilitates profound interactions with water, resulting in the dispersion of the newly functionalized graphene in aqueous solutions. This biofunctionalization method resulted in ≈56% peptide loading on the graphene surface, leading to graphene dispersions that remain stable for months in aqueous solutions outperforming currently used surfactants.

Water-Vapor Responsive Metallo-Peptide Nanofibers.

Short peptides are versatile molecules for the construction of supramolecular materials. Most reported peptide materials are hydrophobic, stiff, and show limited response to environmental conditions in the solid-state. Herein, we describe a design strategy for minimalistic supramolecular metallo-peptide nanofibers that, depending on their sequence, change stiffness, or reversibly assemble in the solid-state, in response to changes in relative humidity (RH). We tested a series of histidine (H) containing dipeptides with varying hydrophobicity, XH, where X is G, A, L, Y (glycine, alanine, leucine, and tyrosine). The one-dimensional fiber formation is supported by metal coordination and dynamic H-bonds. Solvent conditions were identified where GH/Zn and AH/Zn formed gels that upon air-drying gave rise to nanofibers. Upon exposure of the nanofiber networks to increasing RH, a reduction in stiffness was observed with GH/Zn fibers reversibly (dis-)assembled at 60-70 % RH driven by a rebalancing of hydrogen bonding interactions between peptides and water. When these metallo-peptide nanofibers were deposited on the surface of polyimide films and exposed to varying RH, peptide/water-vapor interactions in the solid-state mechanically transferred to the polymer film, leading to the rapid and reversible folding-unfolding of the films, thus demonstrating RH-responsive actuation.