Rosette nanotubes (RNTs) are supramolecular tubular nanostructures assembled from guanine-cytosine-inspired (G∧C) motifs. Building on earlier preliminary studies, we present a comprehensive nanoscale investigation and characterization of peptide-functionalized RNTs as modular scaffolds for programmable surface organization. Three distinct 10-11 amino acid peptides derived from bone morphogenetic protein-7, differing in sequence, charge, and steric bulk, were conjugated to twin G∧C motifs and shown to self-assemble robustly in aqueous media. Using complementary electron microscopy, spectroscopy, and molecular modeling, we elucidate how peptide identity influences nanotube assembly and surface secondary structure. Importantly, we demonstrate controllable coassembly of peptide- and lysine-functionalized motifs, enabling tunable peptide density and spatial distribution along the nanotube surface. This work provides insight into design principles for supramolecular peptide display on nanotubular nanostructures and highlights RNTs as a versatile platform for nanoscale biointerfaces.
Alsbaiee et al. (Mon,) studied this question.