The balance between hydrogen bonding and hydrophobic interactions dictates nanofiber obtained by self‐assembly of many low molecular weight gelators. In here, we demonstrate that thermal history can be used as a simple route of controlling structure and function in supramolecular gels. Using a model aromatic peptide amphiphile, Fmoc‐tyrosyl‐leucine and a combination of fluorescence, FTIR, CD and NMR spectroscopy, we show that the balance of these interactions can be adjusted by varying thermal history followed by supramolecular locking in the gel state. Depending on the thermal history that the gelators are exposed to, three regimes can be identified regarding the balance between H‐bonding and aromatic stacking interactions, resulting in different modes of supramolecular packing. Consequently, non‐equilibrium gels can be obtained with customizable properties, including supramolecular chirality, gel stiffness and proteolytic stability, highlighting the possibility of obtaining a range of supramolecular architectures from a single molecular structure.