Sequence Programming of Electronic Properties in Self-Assembling Peptides

Controlling the electronic properties of peptide materials through molecular sequence remains an outstanding challenge in functional biomaterial design. Here, we establish a sequence-guided framework in which systematic substitution of aromatic residues (phenylalanine, tryptophan, and tyrosine) within an alternating hydrophilic–aromatic peptide motif programs supramolecular assembly and electronic properties. Coarse-grained molecular dynamics reveals that aromatic residue identity governs intermolecular π–π interactions and assembly morphology through distinct packing behavior. Guided by these assembly characteristics, density functional theory predicts sequence-dependent electronic structures and identifies candidate peptides with tunable HOMO–LUMO gaps. Experimental characterization confirms sequence-dependent assembly morphologies by transmission electron microscopy and corresponding differences in electrical conductivity. Together, these results demonstrate that peptide sequence serves as a programmable design parameter linking supramolecular assembly with electronic properties, providing a rational strategy for designing functional peptide electronic materials.