Aromatic Amino Acid-Dependent Surface Assembly of Amphiphilic Peptides for One-Step Graphite Exfoliation and Graphene...

Amphiphilic peptides show great potential for exfoliating graphite and functionalizing graphene. However, the variety of amino acids complicates our understanding of the underlying mechanisms. In this study, we designed four peptides (C6W1, C6W2, C6W4, and C6W6) with different amounts of aromatic tryptophan amino acids and two additional peptides (C6F4 and C6Y4) by substituting tryptophan with aromatic phenylalanine or tyrosine. This allowed us to investigate the processes and mechanisms of graphite exfoliation and graphene functionalization. Using experimental and computational methods, we discovered that peptides containing tryptophan demonstrated higher exfoliation efficiency and increased tryptophan content further improved this efficiency, resulting in more peptide-functionalized graphene layers. Significantly, the primary driving force for the surface-assisted assembly of peptides on graphite is the π-π stacking interaction between the aromatic ring contributed by aromatic amino acids and the hexagonal rings of the graphite surface. This interaction leads to a layer-by-layer exfoliation mechanism. Our research offers valuable insights into peptide design strategies for one-step graphite exfoliation and graphene functionalization in aqueous environments.