Peptide-based self-assembly offers a unique entry into the construction of soft structures with interesting material properties and functions. Aromatic amino acid-containing peptides are commonly employed as they exhibit high propensity to aggregate due to increased hydrophobic content, promotion of favorable secondary structures, planarity and the possibility of π-π interactions. Incorporation of covalent scaffolds, stimuli-responsive handles and carbohydrate moieties augment beneficial characteristics to the resulting peptide conjugates. These modifications were shown to enforce self-association, elicit stimuli response and achieve improved hydrophilic properties, to name but a few.