Figure 2. Supramolecular assemblies of GrBP5-WT peptides on HOPG in aqueous environment. (IMAGE)
Caption
a An overview AFM topography image of peptide nanostructure acquired in PBS buffer, showing long-range order with six-fold symmetric domains that are commensurate with the graphite lattice and b the corresponding 2D-FFT pattern confirming six-fold symmetry. The color scale represents the FFT intensity in arbitrary units. c,d Molecularly resolved AFM images of a stable peptide domain, acquired in PBS buffer, with the panel d showing a zoomed-in view of the framed region. e Crystallographic orientation relationships between peptide crystals and the substrate lattice, defined by matching the peptide molecular lattice to the atomic lattice of the solid, enabling chiral recognition. f Molecular-resolution AFM image of a peptide domain in water. g Simulated structural organization of GrBP5-WT peptide assemblies on graphene. h, i Simulated molecular details show planar alignment of tyrosine (Y) residues in the binding domain enabling π–π stacking with the graphene lattice, while the methionine (M) residue in the IMVT domain protrudes above the surface, enhancing aqueous exposure. j Overlay of the simulated peptide assembly structure onto the AFM image in panel d.
Credit
Yurtsever A., et al., Nat Commun (2026)
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